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2-amino-5-(butan-2-ylamino)-5-oxopentanoic acid
?
-
-
-
-
?
2-amino-5-(cyclohexylamino)-5-oxopentanoic acid
?
-
-
-
-
?
2-amino-5-(cyclopropylamino)-5-oxopentanoic acid
?
-
-
-
-
?
2-amino-5-oxo-5-(propan-2-ylamino)pentanoic acid
?
-
-
-
-
?
2-amino-5-oxo-5-[(2-phenylethyl)amino]pentanoic acid
?
-
-
-
-
?
2-amino-5-[(2-methylbutyl)amino]-5-oxopentanoic acid
?
-
-
-
-
?
2-amino-5-[(2S)-butan-2-ylamino]-5-oxopentanoic acid
?
-
-
-
-
?
2-amino-5-[[(2S)-2-methylbutyl]amino]-5-oxopentanoic acid
?
-
-
-
-
?
39SrpL21 protein
?
-
-
-
?
amyloid beta(3-40)
pyroglutamyl-amyloid beta(3-40) + NH3
-
-
-
-
?
amyloid peptide Abeta(3-40,42)
Abeta(3[pE]-40,42) + H2O
-
-
-
?
amyloid peptide Abeta(3-40/42)
pGluAbeta(3-40/42) + H2O
-
-
significant portion of Abeta peptides of amyloid plaques in Alzheimer's disease brains
-
?
EFRHHDSGYE-NH2
pEFRHHDSGYE-NH2 + H2O
Gln
L-5-oxoproline + NH3
-
-
-
-
?
Gln
pyroglutamate + NH3
-
-
-
-
?
Gln(3)-amyloid-beta peptide 3-11 amide
?
-
-
-
-
?
Gln(3)-amyloid-beta peptide 3-21 amide
?
-
-
-
-
?
Gln(3)-amyloid-beta peptide 3-40 amide
?
-
-
-
-
?
Gln-2-naphthylamide
2-oxoprolyl-2-naphthylamide + NH3
-
-
-
-
?
Gln-2-naphthylamide
pyroglutamyl-2-naphthylamide + NH3
-
-
-
-
?
Gln-4-methylcoumarinylamide
2-oxoprolyl-4-methylcoumarinylamide + NH3
-
-
-
-
?
Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
Gln-7-amido-4-methylcoumarin
pyroglutamic acid-7-amido-4-methylcoumarin + NH3
Gln-Ala
pyroglutamic acid-Ala + NH3
Gln-Ala-Ala-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ala-Ala-NH2 + NH3
Gln-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-NH2 + NH3
Gln-Ala-Ala-Ser-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ser-Ala-Ala-NH2 + NH3
Gln-Arg-Gly-Ile-NH2
pyroglutamic acid-Arg-Gly-Ile-NH2 + NH3
Gln-Arg-Tyr-Phe-NH2
pyroglutamic acid-Arg-Tyr-Phe-NH2 + NH3
Gln-Asn-Gly-Ile-NH2
pyroglutamic acid-Asn-Gly-Ile-NH2 + NH3
Gln-beta-naphthylamide
pyroglutamic acid-beta-naphthylamide + NH3
-
-
-
-
?
Gln-beta-naphthylamide
pyroglutamic acid-beta-naphthylamine + NH3
-
-
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
Gln-Gln
L-5-oxoprolyl-Gln + NH3
-
-
-
-
?
Gln-Gln
pyroglutamic acid-Gln + NH3
Gln-Gln
pyroglutamyl-Gln + NH3
-
-
-
-
?
Gln-Gln-Gln
Glp-Gln-Gln + NH3
Gln-Gln-Tyr-Phe-NH2
pyroglutamic acid-Gln-Tyr-Phe-NH2 + NH3
Gln-Glu
pyroglutamic acid-Glu + NH3
Gln-Glu-Ala-Ala-NH2
pyroglutamic acid-Glu-Ala-Ala-NH2 + NH3
Gln-Glu-Ala-Phe-NH2
pyroglutamic acid-Glu-Ala-Phe-NH2 + NH3
Gln-Glu-Asp-Leu-NH2
pyroglutamic acid-Glu-Asp-Leu-NH2 + NH3
Gln-Glu-Tyr-Ala-NH2
pyroglutamic acid-Glu-Tyr-Ala-NH2 + NH3
Gln-Glu-Tyr-NH2
pyroglutamic acid-Glu-Tyr-NH2 + NH3
Gln-Glu-Tyr-Phe-NH2
pyroglutamic acid-Glu-Tyr-Phe-NH2 + NH3
Gln-Gly
5-oxoprolyl-Gly + NH3
Gln-Gly
pyroglutamic acid-Gly + NH3
Gln-Gly-Pro
Glp-Gly-Pro + NH3
-
-
-
-
?
Gln-Gly-Pro
pGlu-Gly-Pro + NH3
Gln-Gly-Pro
pyroglutamic acid-Gly-Pro + NH3
Gln-His-Pro
pyroglutamyl-His-Pro
-
-
-
-
?
Gln-His-Pro-NH2
L-5-oxoprolyl-His-Pro-NH2 + NH3
-
-
-
-
?
Gln-His-Tyr-Phe-NH2
pyroglutamic acid-His-Tyr-Phe-NH2 + NH3
Gln-Lys-Arg-Leu-NH2
pyroglutamic acid-Lys-Arg-Leu-NH2 + NH3
Gln-Phe-Ala
pGlu-Phe-Ala + NH3
Gln-Phe-Ala-NH2
pyroglutamic acid-Phe-Ala-NH2 + NH3
Gln-Pro-Tyr-Phe-NH2
pyroglutamic acid-Pro-Tyr-Phe-NH2 + NH3
Gln-Ser-Tyr-Phe-NH2
pyroglutamic acid-Ser-Tyr-Phe-NH2 + NH3
Gln-tert-butyl ester
pyroglutamyl-tert-butyl ester + NH3
Gln-Trp-Ala-NH2
pyroglutamic acid-Trp-Ala-NH2 + NH3
Gln-Tyr
pyroglutamic acid-Tyr + NH3
-
-
-
-
?
Gln-Tyr-Ala
pGlu-Tyr-Ala + NH3
Gln-Tyr-Ala
pyroglutamic acid-Tyr-Ala + NH3
Gln-Tyr-Ala-OH
L-5-oxoprolyl-Tyr-Ala + NH3
-
-
-
-
?
Gln-Val
Glp-Val + NH3
-
-
-
-
?
Gln-Val
pyroglutamic acid-Val + NH3
-
-
-
-
?
Glu-2-naphthylamide
?
-
-
-
-
?
glucagon(3-29)
?
-
-
-
-
?
glutamine tert-butyl ester
pyroglutamyl-tert-butyl ester + NH3
-
-
-
-
?
gonadotropin releasing hormone
?
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
H-Gln-7-amido-4-methylcoumarin
? + NH3
H-Gln-Ala-OH
5-oxoprolyl-Ala-OH + NH3
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
H-Gln-Glu-Tyr-Ala-NH2
5-oxoprolyl-Glu-Tyr-Ala-NH2 + NH3
-
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
H-Gln-Phe-Ala-NH2
5-oxoprolyl-Phe-Ala-NH2 + NH3
H-Gln-Phe-Ala-OH
5-oxoprolyl-Phe-Ala-OH + NH3
H-Gln-Phe-Arg-His-NH2
5-oxoprolyl-Phe-Arg-His-NH2 + NH3
-
-
-
-
?
H-Gln-Ser-Tyr-Phe-NH2
5-oxoprolyl-Ser-Tyr-Phe-NH2 + NH3
-
-
-
?
H-Gln-Tyr-Ala-OH
5-oxoprolyl-Tyr-Ala-OH + NH3
H-Gln-Val-Ala-OH
5-oxoprolyl-Val-Ala-OH + NH3
L-gamma-glutamyl-(+)-3-aminobutyric acid
?
-
-
-
-
?
L-gamma-glutamyl-(+)-3-aminoisobutyric acid
?
-
-
-
-
?
L-gamma-glutamyl-beta-alanine
?
-
-
-
-
?
L-gamma-glutamyl-ethylamine
?
-
-
-
-
?
L-gamma-glutamyl-methylamine
?
-
-
-
-
?
L-gamma-glutamyl-n-butylamine
?
-
-
-
-
?
L-gamma-glutamyl-n-propylamine
?
-
-
-
-
?
L-gamma-glutamyl-tert-butylamine
?
-
-
-
-
?
L-gamma-glutamylaniline
?
-
-
-
-
?
L-gamma-glutamylbenzylamine
?
-
-
-
-
?
L-gamma-glutamylcyclopentylamine
?
-
-
-
-
?
L-gamma-glutamylglycine
?
-
poor substrate
-
-
?
L-gamma-glutamylneohexylamine
?
-
-
-
-
?
L-gamma-glutamylneopentylamine
?
-
-
-
-
?
L-Gln(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + NH3
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-4-methylcoumarin-7-amide + NH3
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
L-Gln-7-amido-4-methylcoumarin
pyroglutamate-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-Gln-amide
5-oxoprolyl-amide + NH3
L-Gln-Gly
5-oxoprolyl-Gly + NH3
L-Gln-Gly
5-oxoprolylglycine + NH3
L-Gln-Gly
L-pyroglutamyl-Gly + NH3
L-Gln-Gly-L-Pro
5-oxoprolyl-Gly-L-Pro + NH3
L-Gln-Gly-L-Pro
pyroglutamyl-Gly-L-Pro + NH3
L-Gln-L-Ala
L-pyroglutamyl-L-Ala + NH3
L-Gln-L-Arg-Gly-L-Ile-NH2
pyroglutamyl-L-Arg-Gly-L-Ile-NH2 + NH3
-
-
-
?
L-Gln-L-Asn-Gly-L-Ile-NH2
L-pyroglutamyl-L-Asn-Gly-L-Ile-NH2 + NH3
-
-
-
?
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pyroglutamyl-L-Asp-L-Glu-L-Leu-NH2 + NH3
L-Gln-L-Gln
5-oxoprolyl-L-Gln + NH3
L-Gln-L-Gln
L-pyroglutamyl-L-Gln + NH3
L-Gln-L-Gln-OH
5-oxoprolyl-L-Gln + NH3
-
-
-
?
L-Gln-L-Glu
5-oxoprolyl-L-Glu + NH3
L-Gln-L-Glu
L-pyroglutamyl-L-Glu + NH3
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pyroglutamyl-L-Glu-L-Ala-L-Phe-NH2 + NH3
L-Gln-L-Glu-L-Asp-L-Leu-NH2
5-oxoprolyl-L-Glu-L-Asp-L-Leu-NH2 + NH3
L-Gln-L-Glu-L-Tyr-L-Ala-NH2
pyroglutamic acid-L-Glu-L-Tyr-L-Ala-NH2 + NH3
-
-
-
?
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pyroglutamyl-L-Glu-L-Tyr-L-Phe-NH2 + NH3
L-Gln-L-Glu-OH
5-oxoprolyl-L-Glu + NH3
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu
5-oxoprolyl-L-Lys-L-Arg-L-Leu + NH3
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
5-oxoprolyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pyroglutamyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
L-Gln-L-Phe-L-Ala
5-oxoprolyl-L-Phe-L-Ala + NH3
-
-
-
?
L-Gln-L-Phe-L-Ala-NH2
5-oxoprolyl-L-Phe-L-Ala-NH2 + NH3
L-Gln-L-Phe-L-Ala-NH2
L-pyroglutamyl-L-Phe-L-Ala-NH2 + NH3
L-Gln-L-Ser-L-Tyr-L-Phe-NH2
pyroglutamic acid-L-Ser-L-Tyr-L-Phe-NH2 + NH3
-
-
-
?
L-Gln-L-Thr-Gly-L-Ile-NH2
L-pyroglutamyl-L-Thr-Gly-L-Ile-NH2 + NH3
-
-
-
?
L-Gln-L-Thr-L-Ala
5-oxoprolyl-L-Thr-L-Ala + NH3
-
-
-
-
?
L-Gln-L-Trp-L-Ala-NH2
L-pyroglutamyl-L-Trp-L-Ala-NH2 + NH3
-
-
-
?
L-Gln-L-Val-L-Ala-NH2
L-pyroglutamyl-L-Val-L-Ala-NH2 + NH3
L-Gln-NH2
L-pyroglutamyl amide + NH3
L-Gln-tert-butyl ester
5-oxoprolyl-tert-butyl ester + NH3
L-Gln-tert-butyl ester
L-pyroglutamyl-tert-butyl ester + NH3
L-Glu(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + H2O
L-Glu-2-naphthylamide
5-oxo-L-prolinyl-2-naphthylamide + NH3
-
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolyl-2-naphthylamide + NH3
L-glutamine tert-butyl ester
L-pyroglutamate tert-butyl ester + NH3
-
-
-
-
?
L-glutaminyl 2-naphthylamide
L-glutamine + 2-naphthylamine
-
-
-
?
L-glutaminyl-2-naphthylamide
L-5-oxoprolyl-2-naphthylamide + NH3
-
-
-
-
?
L-glutaminyl-4-methylcoumarinylamide
L-5-oxoprolyl-4-methylcoumarinylamide + NH3
-
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
L-pyroglutamyl-7-amido-4-methylcoumarin + NH3
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
L-glutaminyl-Abeta(3-42) peptide
5-oxoprolyl-Abeta(3-42) peptide + NH3
L-glutaminyl-Abeta3-40/42
5-oxoprolyl-Abeta3-40/42 + NH3
amyloid-beta peptide Abeta3-40/42
-
-
r
L-glutaminyl-Abeta3-40/42 peptide
5-oxoprolyl-Abeta3-40/42 peptide + NH3
amyloid-beta peptide Abeta3-40/42
-
-
?
L-glutaminyl-amyloid beta peptide
5-oxoprolyl-amyloid beta peptide + NH3
L-glutaminyl-beta-naphthylamide
pGlu-beta-naphthylamide + NH3
L-glutaminyl-CCL2
5-oxoprolyl-CCL2 + NH3
L-glutaminyl-CD47
5-oxoprolyl-CD47 + NH3
-
-
-
?
L-glutaminyl-monocyte chemoattractant protein 1
5-oxoprolyl-monocyte chemoattractant protein 1 + NH3
L-glutaminyl-monocyte chemoattractant protein 3
5-oxoprolyl-monocyte chemoattractant protein 3 + NH3
i.e. MCP-3 or CCL7
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
L-glutaminyl-Phe-Ala
5-oxoprolyl-Phe-Ala + NH3
-
-
-
r
Nepsilon-(L-gamma-glutamyl)-D-lysine
?
-
-
-
-
?
Nepsilon-(L-gamma-glutamyl)-L-lysine
5-oxoprolyl-L-lysine + NH3
-
-
-
-
?
O-(n-butylcarbamyl)-L-serine
?
-
-
-
-
?
QAAE
5-oxoprolyl-AAE + NH3
QAAF
5-oxoprolyl-AAF + NH3
QAAR
5-oxoprolyl-AAR + NH3
-
-
-
?
QAEA
5-oxoprolyl-AEA + NH3
QAFA
5-oxoprolyl-AFA + NH3
QARA
5-oxoprolyl-ARA + NH3
QEAA
5-oxoprolyl-EAA + NH3
QFAA
5-oxoprolyl-FAA + NH3
QGGG
5-oxoprolyl-GGG + NH3
QRAA
5-oxoprolyl-RAA + NH3
S-(cyclohexylamine)-L-cysteine
?
-
-
-
-
?
S-(n-butylcarbamyl)-L-cysteine
?
-
-
-
-
?
S-(n-propylcarbamyl)-L-cysteine
?
-
-
-
-
?
thyrotropin-releasing hormone
?
-
-
-
-
?
[Gln1,Gly4]-thyrotropin releasing hormone
?
-
-
-
-
?
[Gln1]-fertilization promoting peptide
[pyroglutamyl]-fertilization promoting peptide + NH3
[Gln1]-gastrin
[pyroglutamyl]-gastrin + NH3
[Gln1]-gonadotropin releasing-hormone
[pyroglutamyl]-gonadotropin releasing-hormone + NH3
[Gln1]-neurotensin
[pyroglutamyl]-neurotensin + NH3
[Gln1]-thyrotropin releasing-hormone
[pyroglutamyl]-thyrotropin releasing-hormone + NH3
-
-
-
-
?
additional information
?
-
EFRH-NH2
pEFRH-NH2 + H2O
-
-
-
-
?
EFRH-NH2
pEFRH-NH2 + H2O
-
-
-
-
?
EFRH-NH2
pEFRH-NH2 + H2O
-
-
-
-
?
EFRH-NH2
pEFRH-NH2 + H2O
-
-
-
-
?
EFRHHDSGYE-NH2
pEFRHHDSGYE-NH2 + H2O
-
-
-
-
?
EFRHHDSGYE-NH2
pEFRHHDSGYE-NH2 + H2O
-
-
-
-
?
EFRHHDSGYE-NH2
pEFRHHDSGYE-NH2 + H2O
-
-
-
-
?
EFRHHDSGYE-NH2
pEFRHHDSGYE-NH2 + H2O
-
-
-
-
?
Gln-7-amido-4-methylcoumarin
pyroglutamic acid-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
Gln-7-amido-4-methylcoumarin
pyroglutamic acid-7-amido-4-methylcoumarin + NH3
-
-
-
?
Gln-Ala
Glp-Ala + NH3
-
-
-
-
?
Gln-Ala
Glp-Ala + NH3
-
-
-
-
?
Gln-Ala
Glp-Ala + NH3
-
-
-
-
?
Gln-Ala
pyroglutamic acid-Ala + NH3
-
-
-
-
?
Gln-Ala
pyroglutamic acid-Ala + NH3
-
-
-
-
?
Gln-Ala-Ala-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Ala-Ala-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Ala-Ala-Ser-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ser-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Ala-Ala-Ser-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ser-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Arg-Gly-Ile-NH2
pyroglutamic acid-Arg-Gly-Ile-NH2 + NH3
-
-
-
-
?
Gln-Arg-Gly-Ile-NH2
pyroglutamic acid-Arg-Gly-Ile-NH2 + NH3
-
-
-
-
?
Gln-Arg-Tyr-Phe-NH2
pyroglutamic acid-Arg-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Arg-Tyr-Phe-NH2
pyroglutamic acid-Arg-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Asn-Gly-Ile-NH2
pyroglutamic acid-Asn-Gly-Ile-NH2 + NH3
-
-
-
-
?
Gln-Asn-Gly-Ile-NH2
pyroglutamic acid-Asn-Gly-Ile-NH2 + NH3
-
-
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
-
-
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
-
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
isoDromeQC
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
-
-
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
-
-
-
-
?
Gln-Gln
5-oxoprolyl-Gln + NH3
-
-
-
?
Gln-Gln
Glp-Gln + NH3
-
-
-
-
?
Gln-Gln
Glp-Gln + NH3
-
-
-
-
?
Gln-Gln
Glp-Gln + NH3
-
-
-
-
?
Gln-Gln
Glp-Gln + NH3
-
-
-
?
Gln-Gln
pGlu-Gln + NH3
-
-
-
-
?
Gln-Gln
pGlu-Gln + NH3
-
-
-
-
?
Gln-Gln
pyroglutamic acid-Gln + NH3
-
-
-
-
?
Gln-Gln
pyroglutamic acid-Gln + NH3
-
-
-
-
?
Gln-Gln
pyroglutamic acid-Gln + NH3
-
-
-
?
Gln-Gln-Gln
Glp-Gln-Gln + NH3
-
-
-
-
?
Gln-Gln-Gln
Glp-Gln-Gln + NH3
-
-
-
-
?
Gln-Gln-Gln
Glp-Gln-Gln + NH3
-
-
-
-
?
Gln-Gln-Tyr-Phe-NH2
pyroglutamic acid-Gln-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Gln-Tyr-Phe-NH2
pyroglutamic acid-Gln-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Glu
Glp-Glu + NH3
-
-
-
-
?
Gln-Glu
Glp-Glu + NH3
-
-
-
-
?
Gln-Glu
pGlu-Glu + NH3
-
-
-
-
?
Gln-Glu
pGlu-Glu + NH3
-
-
-
-
?
Gln-Glu
pyroglutamic acid-Glu + NH3
-
-
-
-
?
Gln-Glu
pyroglutamic acid-Glu + NH3
-
-
-
-
?
Gln-Glu-Ala-Ala-NH2
pyroglutamic acid-Glu-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Glu-Ala-Ala-NH2
pyroglutamic acid-Glu-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Glu-Ala-Phe-NH2
pyroglutamic acid-Glu-Ala-Phe-NH2 + NH3
-
-
-
-
?
Gln-Glu-Ala-Phe-NH2
pyroglutamic acid-Glu-Ala-Phe-NH2 + NH3
-
-
-
-
?
Gln-Glu-Asp-Leu-NH2
pyroglutamic acid-Glu-Asp-Leu-NH2 + NH3
-
-
-
-
?
Gln-Glu-Asp-Leu-NH2
pyroglutamic acid-Glu-Asp-Leu-NH2 + NH3
-
-
-
-
?
Gln-Glu-Tyr-Ala-NH2
pyroglutamic acid-Glu-Tyr-Ala-NH2 + NH3
-
-
-
-
?
Gln-Glu-Tyr-Ala-NH2
pyroglutamic acid-Glu-Tyr-Ala-NH2 + NH3
-
-
-
-
?
Gln-Glu-Tyr-NH2
pyroglutamic acid-Glu-Tyr-NH2 + NH3
-
-
-
-
?
Gln-Glu-Tyr-NH2
pyroglutamic acid-Glu-Tyr-NH2 + NH3
-
-
-
-
?
Gln-Glu-Tyr-Phe-NH2
pyroglutamic acid-Glu-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Glu-Tyr-Phe-NH2
pyroglutamic acid-Glu-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
-
?
Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
?
Gln-Gly
5-oxoprolyl-Gly + NH3
isoDromeQC
-
-
?
Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
-
?
Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
-
?
Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
?
Gln-Gly
Glp-Gly + NH3
-
-
-
-
?
Gln-Gly
Glp-Gly + NH3
-
-
-
-
?
Gln-Gly
Glp-Gly + NH3
-
-
-
-
?
Gln-Gly
pGlu-Gly + NH3
-
-
-
-
?
Gln-Gly
pGlu-Gly + NH3
-
-
-
-
?
Gln-Gly
pyroglutamic acid-Gly + NH3
-
-
-
-
?
Gln-Gly
pyroglutamic acid-Gly + NH3
-
-
-
-
?
Gln-Gly-Pro
pGlu-Gly-Pro + NH3
-
-
-
-
?
Gln-Gly-Pro
pGlu-Gly-Pro + NH3
-
-
-
-
?
Gln-Gly-Pro
pyroglutamic acid-Gly-Pro + NH3
-
-
-
-
?
Gln-Gly-Pro
pyroglutamic acid-Gly-Pro + NH3
-
-
-
-
?
Gln-His-Tyr-Phe-NH2
pyroglutamic acid-His-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-His-Tyr-Phe-NH2
pyroglutamic acid-His-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Lys-Arg-Leu-NH2
pyroglutamic acid-Lys-Arg-Leu-NH2 + NH3
-
-
-
-
?
Gln-Lys-Arg-Leu-NH2
pyroglutamic acid-Lys-Arg-Leu-NH2 + NH3
-
-
-
-
?
Gln-NH2
Glp-amide + NH3
-
-
-
-
?
Gln-NH2
Glp-amide + NH3
-
-
-
-
?
Gln-NH2
Glp-amide + NH3
-
-
-
-
?
Gln-Phe-Ala
pGlu-Phe-Ala + NH3
-
-
-
-
?
Gln-Phe-Ala
pGlu-Phe-Ala + NH3
-
-
-
-
?
Gln-Phe-Ala-NH2
pyroglutamic acid-Phe-Ala-NH2 + NH3
-
-
-
-
?
Gln-Phe-Ala-NH2
pyroglutamic acid-Phe-Ala-NH2 + NH3
-
-
-
-
?
Gln-Pro-Tyr-Phe-NH2
pyroglutamic acid-Pro-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Pro-Tyr-Phe-NH2
pyroglutamic acid-Pro-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Ser-Tyr-Phe-NH2
pyroglutamic acid-Ser-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-Ser-Tyr-Phe-NH2
pyroglutamic acid-Ser-Tyr-Phe-NH2 + NH3
-
-
-
-
?
Gln-tert-butyl ester
pyroglutamyl-tert-butyl ester + NH3
-
-
-
-
?
Gln-tert-butyl ester
pyroglutamyl-tert-butyl ester + NH3
-
-
-
-
?
Gln-Trp-Ala-NH2
pyroglutamic acid-Trp-Ala-NH2 + NH3
-
-
-
-
?
Gln-Trp-Ala-NH2
pyroglutamic acid-Trp-Ala-NH2 + NH3
-
-
-
-
?
Gln-Tyr-Ala
pGlu-Tyr-Ala + NH3
-
-
-
-
?
Gln-Tyr-Ala
pGlu-Tyr-Ala + NH3
-
-
-
-
?
Gln-Tyr-Ala
pyroglutamic acid-Tyr-Ala + NH3
-
-
-
-
?
Gln-Tyr-Ala
pyroglutamic acid-Tyr-Ala + NH3
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
? + NH3
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
? + NH3
-
-
-
?
H-Gln-Ala-OH
5-oxoprolyl-Ala-OH + NH3
-
-
-
-
?
H-Gln-Ala-OH
5-oxoprolyl-Ala-OH + NH3
-
-
-
?
H-Gln-Ala-OH
5-oxoprolyl-Ala-OH + NH3
isoDromeQC
-
-
?
H-Gln-Ala-OH
5-oxoprolyl-Ala-OH + NH3
-
-
-
?
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
-
-
-
-
?
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
-
-
-
?
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
-
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
-
-
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
-
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
isoDromeQC
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
-
-
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
-
-
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
-
-
-
?
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
-
-
-
-
?
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
-
-
-
?
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
-
-
-
?
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
-
-
-
-
?
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
-
-
-
?
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
isoDromeQC
-
-
?
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
-
-
-
-
?
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
-
-
-
-
?
H-Gln-Glu-OH
5-oxoprolyl-Glu-OH + NH3
-
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
-
-
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
-
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
-
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
-
-
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
-
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
isoDromeQC
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
-
-
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
-
-
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
-
-
-
?
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
-
-
-
-
?
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
-
-
-
?
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
-
-
-
?
H-Gln-NH2
? + NH3
-
-
-
-
?
H-Gln-NH2
? + NH3
-
-
-
?
H-Gln-Phe-Ala-NH2
5-oxoprolyl-Phe-Ala-NH2 + NH3
-
-
-
-
?
H-Gln-Phe-Ala-NH2
5-oxoprolyl-Phe-Ala-NH2 + NH3
-
-
-
?
H-Gln-Phe-Ala-OH
5-oxoprolyl-Phe-Ala-OH + NH3
-
-
-
?
H-Gln-Phe-Ala-OH
5-oxoprolyl-Phe-Ala-OH + NH3
isoDromeQC
-
-
?
H-Gln-Tyr-Ala-OH
5-oxoprolyl-Tyr-Ala-OH + NH3
-
-
-
?
H-Gln-Tyr-Ala-OH
5-oxoprolyl-Tyr-Ala-OH + NH3
isoDromeQC
-
-
?
H-Gln-Val-Ala-OH
5-oxoprolyl-Val-Ala-OH + NH3
-
-
-
-
?
H-Gln-Val-Ala-OH
5-oxoprolyl-Val-Ala-OH + NH3
-
-
-
?
H-Gln-Val-Ala-OH
5-oxoprolyl-Val-Ala-OH + NH3
isoDromeQC
-
-
?
H-Gln-Val-Ala-OH
5-oxoprolyl-Val-Ala-OH + NH3
-
-
-
?
L-Gln(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + NH3
-
-
-
-
?
L-Gln(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + NH3
-
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
-
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
reaction in cell supernatant is exclusively enzyme-catalyzed
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
reaction in cell supernatant is exclusively enzyme-catalyzed
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-4-methylcoumarin-7-amide + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-4-methylcoumarin-7-amide + NH3
isoDromeQC
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
?
L-Gln-amide
5-oxoprolyl-amide + NH3
-
-
-
?
L-Gln-amide
5-oxoprolyl-amide + NH3
-
-
-
?
L-Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
?
L-Gln-Gly
5-oxoprolyl-Gly + NH3
-
-
-
?
L-Gln-Gly
5-oxoprolylglycine + NH3
-
-
-
?
L-Gln-Gly
5-oxoprolylglycine + NH3
-
-
-
?
L-Gln-Gly
L-pyroglutamyl-Gly + NH3
-
-
-
-
?
L-Gln-Gly
L-pyroglutamyl-Gly + NH3
-
-
-
?
L-Gln-Gly
L-pyroglutamyl-Gly + NH3
-
-
-
?
L-Gln-Gly-L-Pro
5-oxoprolyl-Gly-L-Pro + NH3
-
-
-
?
L-Gln-Gly-L-Pro
5-oxoprolyl-Gly-L-Pro + NH3
-
-
-
?
L-Gln-Gly-L-Pro
5-oxoprolyl-Gly-L-Pro + NH3
-
-
-
?
L-Gln-Gly-L-Pro
pyroglutamyl-Gly-L-Pro + NH3
-
-
-
-
?
L-Gln-Gly-L-Pro
pyroglutamyl-Gly-L-Pro + NH3
-
-
-
?
L-Gln-Gly-L-Pro
pyroglutamyl-Gly-L-Pro + NH3
-
-
-
?
L-Gln-L-Ala
L-pyroglutamyl-L-Ala + NH3
-
-
-
-
?
L-Gln-L-Ala
L-pyroglutamyl-L-Ala + NH3
-
-
-
?
L-Gln-L-Ala
L-pyroglutamyl-L-Ala + NH3
-
-
-
?
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pyroglutamyl-L-Asp-L-Glu-L-Leu-NH2 + NH3
-
-
-
-
?
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pyroglutamyl-L-Asp-L-Glu-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Gln
5-oxoprolyl-L-Gln + NH3
-
-
-
?
L-Gln-L-Gln
5-oxoprolyl-L-Gln + NH3
-
-
-
?
L-Gln-L-Gln
5-oxoprolyl-L-Gln + NH3
-
-
-
?
L-Gln-L-Gln
L-pyroglutamyl-L-Gln + NH3
-
-
-
-
?
L-Gln-L-Gln
L-pyroglutamyl-L-Gln + NH3
-
-
-
?
L-Gln-L-Gln
L-pyroglutamyl-L-Gln + NH3
-
-
-
?
L-Gln-L-Glu
5-oxoprolyl-L-Glu + NH3
-
-
-
?
L-Gln-L-Glu
5-oxoprolyl-L-Glu + NH3
-
-
-
?
L-Gln-L-Glu
5-oxoprolyl-L-Glu + NH3
-
-
-
?
L-Gln-L-Glu
L-pyroglutamyl-L-Glu + NH3
-
-
-
-
?
L-Gln-L-Glu
L-pyroglutamyl-L-Glu + NH3
-
-
-
?
L-Gln-L-Glu
L-pyroglutamyl-L-Glu + NH3
-
-
-
?
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pyroglutamyl-L-Glu-L-Ala-L-Phe-NH2 + NH3
-
-
-
-
?
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pyroglutamyl-L-Glu-L-Ala-L-Phe-NH2 + NH3
-
-
-
?
L-Gln-L-Glu-L-Asp-L-Leu-NH2
5-oxoprolyl-L-Glu-L-Asp-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Glu-L-Asp-L-Leu-NH2
5-oxoprolyl-L-Glu-L-Asp-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pyroglutamyl-L-Glu-L-Tyr-L-Phe-NH2 + NH3
-
-
-
-
?
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pyroglutamyl-L-Glu-L-Tyr-L-Phe-NH2 + NH3
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
5-oxoprolyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
5-oxoprolyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pyroglutamyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
-
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pyroglutamyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Phe-L-Ala-NH2
5-oxoprolyl-L-Phe-L-Ala-NH2 + NH3
-
-
-
?
L-Gln-L-Phe-L-Ala-NH2
5-oxoprolyl-L-Phe-L-Ala-NH2 + NH3
-
-
-
?
L-Gln-L-Phe-L-Ala-NH2
L-pyroglutamyl-L-Phe-L-Ala-NH2 + NH3
-
-
-
-
?
L-Gln-L-Phe-L-Ala-NH2
L-pyroglutamyl-L-Phe-L-Ala-NH2 + NH3
-
-
-
?
L-Gln-L-Val-L-Ala-NH2
L-pyroglutamyl-L-Val-L-Ala-NH2 + NH3
-
-
-
-
?
L-Gln-L-Val-L-Ala-NH2
L-pyroglutamyl-L-Val-L-Ala-NH2 + NH3
-
-
-
?
L-Gln-NH2
L-pyroglutamyl amide + NH3
-
-
-
-
?
L-Gln-NH2
L-pyroglutamyl amide + NH3
-
-
-
-
?
L-Gln-NH2
L-pyroglutamyl amide + NH3
-
-
-
-
?
L-Gln-NH2
L-pyroglutamyl amide + NH3
-
-
-
?
L-Gln-tert-butyl ester
5-oxoprolyl-tert-butyl ester + NH3
-
-
-
?
L-Gln-tert-butyl ester
5-oxoprolyl-tert-butyl ester + NH3
-
-
-
?
L-Gln-tert-butyl ester
L-pyroglutamyl-tert-butyl ester + NH3
-
-
-
-
?
L-Gln-tert-butyl ester
L-pyroglutamyl-tert-butyl ester + NH3
-
-
-
?
L-Glu(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + H2O
-
-
-
-
?
L-Glu(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + H2O
-
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolyl-2-naphthylamide + NH3
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolyl-2-naphthylamide + NH3
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolyl-2-naphthylamide + NH3
-
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
L-pyroglutamyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
L-pyroglutamyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-glutaminyl-Abeta(3-42) peptide
5-oxoprolyl-Abeta(3-42) peptide + NH3
-
-
-
?
L-glutaminyl-Abeta(3-42) peptide
5-oxoprolyl-Abeta(3-42) peptide + NH3
a glutamate residue (E) is exposed at position 3 of Abeta(3-42) and can be converted by the enzymatic activity of glutaminyl cyclase (QC) to pE resulting in the peptide pE-Abeta(3-42). 5-Oxoproline ring formation under liberation of water. Slow conversion of N-terminal glutamate under slightly acidic pH conditions, as compared with the much faster pE formation from N-terminal glutamine
-
-
?
L-glutaminyl-amyloid beta peptide
5-oxoprolyl-amyloid beta peptide + NH3
-
-
-
-
?
L-glutaminyl-amyloid beta peptide
5-oxoprolyl-amyloid beta peptide + NH3
-
-
-
-
?
L-glutaminyl-beta-naphthylamide
pGlu-beta-naphthylamide + NH3
-
-
-
-
?
L-glutaminyl-beta-naphthylamide
pGlu-beta-naphthylamide + NH3
-
-
-
-
?
L-glutaminyl-CCL2
5-oxoprolyl-CCL2 + NH3
i.e. monocyte chemoattractant protein (MCP-1)
-
-
r
L-glutaminyl-CCL2
5-oxoprolyl-CCL2 + NH3
i.e. monocyte chemoattractant protein (MCP-1), CCL2 is a specific substrate for h-isoQC but not for h-QC
-
-
r
L-glutaminyl-monocyte chemoattractant protein 1
5-oxoprolyl-monocyte chemoattractant protein 1 + NH3
i.e. MCP-1 or CCL2
-
-
?
L-glutaminyl-monocyte chemoattractant protein 1
5-oxoprolyl-monocyte chemoattractant protein 1 + NH3
-
i.e. MCP-1 or CCL2
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
Gln-His-Pro-Glythyrotropin-releasing hormone, gonadotropin-releasing hormone and L-Gln-Tyr-Ala
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
the enzyme may participate in the posttranslational processing of hormonal precursors to pyroglutamyl peptides
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
simple intramolecular cyclization. The mechanism consists of the following main steps: 1. intramolecular nucleophilic attack on the gamma-C=O carbon by the nitrogen of the alpha-amino group, 2. transfer of a proton from the alpha-amino group to the nitrogen of the amide group, facilitated by an acidic group of the enzyme, 3. expulsion of the ammonia-leaving group promoted by this or another acidic enzyme group
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
r
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
the N-terminal formation of 5-oxoproline is a common post-translational event during biosynthesis of a number of peptides
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
Gln-His-Pro-Glythyrotropin-releasing hormone, gonadotropin-releasing hormone and L-Gln-Tyr-Ala
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
QAAE
5-oxoprolyl-AAE + NH3
-
-
-
?
QAAE
5-oxoprolyl-AAE + NH3
-
-
-
?
QAAF
5-oxoprolyl-AAF + NH3
-
-
-
?
QAAF
5-oxoprolyl-AAF + NH3
-
-
-
?
QAEA
5-oxoprolyl-AEA + NH3
-
-
-
?
QAEA
5-oxoprolyl-AEA + NH3
-
-
-
?
QAFA
5-oxoprolyl-AFA + NH3
-
-
-
?
QAFA
5-oxoprolyl-AFA + NH3
-
-
-
?
QARA
5-oxoprolyl-ARA + NH3
-
-
-
?
QARA
5-oxoprolyl-ARA + NH3
-
-
-
?
QEAA
5-oxoprolyl-EAA + NH3
-
-
-
?
QEAA
5-oxoprolyl-EAA + NH3
-
-
-
?
QEDL
pEEDL + NH3
-
-
-
-
?
QEDL
pEEDL + NH3
-
-
-
-
?
QEYF
pEEYF + NH3
-
-
-
-
?
QEYF
pEEYF + NH3
-
-
-
-
?
QFAA
5-oxoprolyl-FAA + NH3
-
-
-
?
QFAA
5-oxoprolyl-FAA + NH3
-
-
-
?
QFRH-NH2
pEFRH-NH2 + NH3
-
-
-
-
?
QFRH-NH2
pEFRH-NH2 + NH3
-
-
-
-
?
QFRH-NH2
pEFRH-NH2 + NH3
-
-
-
-
?
QFRH-NH2
pEFRH-NH2 + NH3
-
-
-
-
?
QGGG
5-oxoprolyl-GGG + NH3
-
-
-
?
QGGG
5-oxoprolyl-GGG + NH3
-
-
-
?
QRAA
5-oxoprolyl-RAA + NH3
-
-
-
?
QRAA
5-oxoprolyl-RAA + NH3
-
-
-
?
[Gln1]-fertilization promoting peptide
[pyroglutamyl]-fertilization promoting peptide + NH3
-
-
-
-
?
[Gln1]-fertilization promoting peptide
[pyroglutamyl]-fertilization promoting peptide + NH3
-
-
-
-
?
[Gln1]-gastrin
[pyroglutamyl]-gastrin + NH3
-
-
-
-
?
[Gln1]-gastrin
[pyroglutamyl]-gastrin + NH3
-
-
-
-
?
[Gln1]-gonadotropin releasing-hormone
[pyroglutamyl]-gonadotropin releasing-hormone + NH3
-
-
-
-
?
[Gln1]-gonadotropin releasing-hormone
[pyroglutamyl]-gonadotropin releasing-hormone + NH3
-
-
-
-
?
[Gln1]-neurotensin
[pyroglutamyl]-neurotensin + NH3
-
-
-
-
?
[Gln1]-neurotensin
[pyroglutamyl]-neurotensin + NH3
-
-
-
-
?
additional information
?
-
-
highest specificities are observed with substrates possessing large hydrophobic residues adjacent to the N-terminal glutamine and for fluorogenic dipeptide surrogates. Enzyme also catalyzes the conversion of N-terminal glutamic acid residues to pyroglutamic acid, but with about 100000fold lower specificity
-
-
?
additional information
?
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
?
additional information
?
-
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
?
additional information
?
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
?
additional information
?
-
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
?
additional information
?
-
-
no substrates are D-Gln-Tyr-Ala and Lys-Arg-Gln-His-Pro-Gly-Lys-Arg, i.e. thyrotropin releasing hormone precursor
-
-
?
additional information
?
-
-
Cys residues do not participate to the catalytic events
-
-
?
additional information
?
-
-
the second amino acid residue in N-terminal glutaminyl peptides significantly accelerates activity while the third residue provides no further rate enhancement. Substrate binding is the main specificity-determining step
-
-
?
additional information
?
-
-
the enzyme may play a key role in posttranslational modification
-
-
?
additional information
?
-
-
the enzyme may play a key role in posttranslational modification
-
-
?
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
?
additional information
?
-
-
catalyzes the formation of amyloid-beta3(pE)-40/42 after amyloidogenic processing of amyloid precursor protein
-
-
?
additional information
?
-
orexin A, gastrin, gonadotropin, TRH, MCP-1 to 4, FPP, fibronectin, and neurotensin are substrates of the enzyme
-
-
-
additional information
?
-
cyclization reaction of glutamate and glutamine residues, overview
-
-
-
additional information
?
-
cyclization reaction of glutamate and glutamine residues, overview
-
-
-
additional information
?
-
cyclization reaction of glutamate and glutamine residues, overview. CCL2 is a specific substrate for h-isoQC but not for h-QC
-
-
-
additional information
?
-
cyclization reaction of glutamate and glutamine residues, overview. CCL2 is a specific substrate for h-isoQC but not for h-QC
-
-
-
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
?
additional information
?
-
the enzyme shows no activity towards L-Gln-Gly
-
-
?
additional information
?
-
-
the enzyme does not act on L-2-amino-3-(3-n-butylureido)-propionic acid, L-glutamine, L-gamma-glutamyl-L-lysine, L-gamma-glutamyl-L-methionine, or L-gamma-glutamyl-L-glutamine
-
-
?
additional information
?
-
-
no substrates are D-Gln-Tyr-Ala and Lys-Arg-Gln-His-Pro-Gly-Lys-Arg, i.e. thyrotropin releasing hormone precursor
-
-
?
additional information
?
-
-
highest specificities are observed with substrates possessing large hydrophobic residues adjacent to the N-terminal glutamine and for fluorogenic dipeptide surrogates. Enzyme also catalyzes the conversion of N-terminal glutamic acid residues to pyroglutamic acid, but with about 100000fold lower specificity
-
-
?
additional information
?
-
highest specificities are observed with substrates possessing large hydrophobic residues adjacent to the N-terminal glutamine and for fluorogenic dipeptide surrogates. Enzyme also catalyzes the conversion of N-terminal glutamic acid residues to pyroglutamic acid, but with about 100000fold lower specificity
-
-
?
additional information
?
-
the enzyme shows no activity towards QAAR
-
-
?
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(3,4-dichlorophenyl)-2-cyano-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(3,4-dimethoxyphenyl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(4-(trifluoromethyl)phenyl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(4-isopropylphenyl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(4-methoxyphenyl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(cyclopropylmethyl)guanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-methylguanidine
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-phenylguanidine
-
(3-(1H-imidazol-1-yl)propyl)-3-(4-bromophenyl)-2-cyanoguanidine
-
(3-(4-methyl-1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
(E)-N1-(5-methyl-1H-imidazol-1-yl)-2-nitro-N'1-[4-(trifluoromethyl)phenyl]ethene-1,1-diamine
-
1,2-di-O-palmitoyl-3-O-(6'-deoxy-6'-sulfo-D-glycopyranosyl)-glycerol
1,4-bis-(imidazol-1-yl)methyl-2,5-dimethylbenzene
-
1-(2,3-dihydro-1,4-benzodioxin-6-yl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(2,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(2-oxo-2-phenylethyl)-imidazole
-
1-(3,4-dimethoxybenzyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(3,4-dimethoxyphenyl)-3-(2-[1-(1H-imidazol-1-yl)cyclopropyl]ethyl)thiourea
-
-
1-(3,4-dimethoxyphenyl)-3-(3-(4-methyl-1H-imidazol-1-yl)propyl)thiourea
-
1-(3,4-dimethoxyphenyl)-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
1-(3,4-dimethoxyphenyl)-3-[(3R)-3-(1H-imidazol-1-yl)butyl]thiourea
-
-
1-(3,4-dimethoxyphenyl)-3-[(3S)-3-(1H-imidazol-1-yl)butyl]thiourea
-
-
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]urea
-
-
1-(3,4-dimethoxyphenyl)-3-[4-(1H-imidazol-1-yl)butyl]thiourea
-
-
1-(3,4-dimethoxyphenyl)-N-(1H-imidazol-1-yl)cyclopropane-1-carbothioamide
-
1-(3,4-dimethoxyphenyl)-N-(3-(4-methyl-1H-imidazol-1-yl)propyl)cyclopropanecarbothioamide
-
1-(3,4-dimethoxyphenyl)-N-(3-(5-methyl-1H-imidazol-1-yl)propyl)cyclopropanecarbothioamide
-
1-(3,4-dimethoxyphenyl)-N-(4-methyl-1H-imidazol-1-yl)cyclopropane-1-carbothioamide
-
1-(3,4-dimethoxyphenyl)-N-(5-methyl-1H-imidazol-1-yl)cyclopropane-1-carbothioamide
-
1-(3,4-dimethoxyphenyl)-N-[3-(1H-imidazol-1-yl)propyl]cyclopropane-1-carbothioamide
-
1-(3,5-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(3-aminopropyl)-imidazole
-
1-(4-acetylphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(4-ethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(4-ethylphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(6-phenoxyhexyl)-1H-imidazole
-
1-methyl-4-(beta-aminoethyl)-imidazole
-
1-methyl-5-(beta-aminoethyl)-imidazole
-
1-O-linolyl-2-O-palmitoyl-3-O-(6'-deoxy-6'-sulfo-D-glucopyranosyl)-glycerol
1-O-palmitoyl-2-O-linolenyl-3-O-(6'-deoxy-6'-sulfo-D-glucopyranosyl)-glycerol
1-[3-(1H-imidazol-1-yl)propyl]-3-(1-naphthyl)thiourea
-
-
1-[3-(1H-imidazol-1-yl)propyl]-3-(3,4,5-trimethoxyphenyl)thiourea
-
-
1-[3-(1H-imidazol-1-yl)propyl]-3-(3-methoxyphenyl)thiourea
-
-
1-[3-(1H-imidazol-1-yl)propyl]-3-(4-methoxyphenyl)thiourea
-
-
1-[3-(1H-imidazol-1-yl)propyl]-3-(4-methylphenyl)thiourea
-
-
1-[3-(1H-imidazol-1-yl)propyl]-3-[4-(methylthio)phenyl]thiourea
-
-
1-[4-(benzyloxy)phenyl]-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
2,3-dihydro-3-(3-(4-methyl-1H-imidazol-1-yl)propyl)-2-thioxoquinazolin-4(1H)-one
-
2,3-dihydro-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-thioxoquinazolin-4(1H)-one
-
2,3-dihydro-6-methyl-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-5-phenyl-2-thioxothieno[2,3-d]pyrimidin-4(1H)-one
-
2,6-dipicolinic acid
time-dependent inactivation
2-(2,3-dimethoxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
87.7% inhibition at 0.1 mM
2-(2,3-dimethoxyphenyl)-7-hydroxy-4H-chromen-4-one
54.3% inhibition at 0.1 mM
2-(2,4-dimethoxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
71.7% inhibition at 0.1 mM
2-(2-fluorophenyl)-5,7-dihydroxy-4H-chromen-4-one
84.2% inhibition at 0.1 mM
2-(2-fluorophenyl)-7-hydroxy-4H-chromen-4-one
60.8% inhibition at 0.1 mM
2-(3,4-dimethoxyphenyl)-7-hydroxy-4H-chromen-4-one
68.3% inhibition at 0.1 mM
2-(3-fluorophenyl)-7-hydroxy-4H-chromen-4-one
63.3% inhibition at 0.1 mM
2-(4-(dimethylamino)phenyl)-7-hydroxy-4H-chromen-4-one
90.3% inhibition at 0.1 mM
2-(4-ethoxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
2-(4-ethoxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
91.5% inhibition at 0.1 mM
2-(4-ethoxyphenyl)-7-hydroxy-4H-chromen-4-one
67.6% inhibition at 0.1 mM
2-(4-ethylphenyl)-5,7-dihydroxy-4H-chromen-4-one
85.2% inhibition at 0.1 mM
2-(4-ethylphenyl)-7-hydroxy-4H-chromen-4-one
79.5% inhibition at 0.1 mM
2-(4-fluorophenyl)-7-hydroxy-4H-chromen-4-one
74.2% inhibition at 0.1 mM
2-(furan-2-yl)-7-hydroxy-4H-chromen-4-one
68.7% inhibition at 0.1 mM
2-(furan-3-yl)-7-hydroxy-4H-chromen-4-one
61.4% inhibition at 0.1 mM
2-cyano(3,4,5-trimethoxyphenyl)-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)guanidine
-
2-cyano(3-(5-methyl-1H-imidazol-1-yl)propyl)-3-(3,4-dimethylphenyl)guanidine
-
2-cyano-1-[3-(5-methyl-1H-imidazol-1-yl)propyl]-4-phenylbenzene-1-guanidine
-
2-ethyl-4-methyl-imidazole
-
2-methyl-benzylimidazole
-
3,5-diamino-1,2-S4-triazole
-
0.14 mM, 10% inhibition
3-(3-(1H-imidazol-1-yl)propyl)-2,3-dihydro-2-thioxoquinazolin-4(1H)-one
-
3-(3-(1H-imidazol-1-yl)propyl)-2,3-dihydro-7-methyl-2-thioxothieno[3,2-d]pyrimidin-4(1H)-one
-
3-(5-methyl-1H-imidazol-1-yl)-6-phenyl-2-sulfanylidene-2,3-dihydrothieno[2,3-d]pyrimidin-4(1H)-one
-
3-Amino-1,2,4-triazole
-
0.14 mM, 15% inhibition
3-fluoro-3',4'-dimethoxy-N-[3-(4-methyl-1H-imidazol-1-yl)propyl][1,1'-biphenyl]-2-amine
-
3-[(1H-imidazol-1-yl)methyl]aniline
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-1,2,3,5,6,7-hexahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8,9,10-octahydrocycloocta[4,5]thieno[2,3-d]pyrimidin-4(1H)-one
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxoimidazolidin-4-one
-
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-sulfanylidene-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-sulfanylidene-2,3-dihydroquinazolin-4(1H)-one
-
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8,9,10-octahydrocycloocta[4,5]-thieno[2,3-d]pyrimidin-4(1H)-one
-
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
3-[4-(1H-imidazol-1-yl)butoxy]benzaldehyde
-
4'-fluoro-N-[3-(4-methyl-1H-imidazol-1-yl)propyl][1,1'-biphenyl]-2-amine
-
4-(2-imidazol-1-yl-ethoxy)-benzoic acid
-
4-imidazole-carboxaldehyde
-
4-phenyl-1,2,4-triazoleine-3,5-dione
-
0.14 mM, 22% inhibition
4-[2-(1H-imidazol-1-yl)ethoxy]benzaldehyde
-
4-[2-[4-([1-[(3-aminophenyl)methyl]-1H-imidazol-2-yl]methyl)-1H-imidazol-1-yl]ethoxy]benzaldehyde
-
5,6-dimethoxy-N-(3-(5-methyl-1H-imidazol-1-yl)propyl)-1Hbenzo[d]imidazol-2-amine
-
5,6-dimethoxy-N-[3-(5-methyl-1H-imidazol-1-yl)propyl]-1,3-benzothiazol-2-amine
-
5,6-dimethoxy-N-[3-(5-methyl-1H-imidazol-1-yl)propyl]-1H-benzimidazol-2-amine
-
5,7-dihydroxy-2-(3-methylphenyl)-4H-1-benzopyran-4-one
-
5,7-dihydroxy-2-(3-methylthiophen-2-yl)-4H-chromen-4-one
91.6% inhibition at 0.1 mM
5,7-dihydroxy-2-(5-methylthiophen-2-yl)-4H-1-benzopyran-4-one
-
5,7-dihydroxy-2-(5-methylthiophen-2-yl)-4H-chromen-4-one
92.4% inhibition at 0.1 mM
5,7-dihydroxy-2-(m-tolyl)-4H-chromen-4-one
93.0% inhibition at 0.1 mM
5,7-dihydroxy-2-(thiophen-2-yl)-4H-1-benzopyran-4-one
-
5,7-dihydroxy-2-(thiophen-2-yl)-4H-chromen-4-one
92.6% inhibition at 0.1 mM
5-(5-[[(3,4-dimethoxyphenyl)sulfanyl]methyl]-1,3,4-oxadiazol-2-yl)-1H-benzimidazole
-
5-(5-[[(pyridin-4-yl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)-1H-benzimidazole
-
5-(methylthio)-1-H-tetrazole
-
0.14 mM, 11% inhibition
5-amino-3H-imidazole-4-carboxylic acid amide
-
5-hydroxymethyl-4-methyl-imidazole
-
5-[5-(2-phenylethyl)-1,3,4-oxadiazol-2-yl]-1H-benzimidazole
-
6-benzyl-2,3-dihydro-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-thioxothieno[2,3-d]pyrimidin-4(1H)-one
-
7-hydroxy-2-(2-(trifluoromethyl)phenyl)-4H-chromen-4-one
70.8% inhibition at 0.1 mM
7-hydroxy-2-(2-methoxyphenyl)-4H-chromen-4-one
54.5% inhibition at 0.1 mM
7-hydroxy-2-(3,4,5-trimethoxyphenyl)-4H-chromen-4-one
68.7% inhibition at 0.1 mM
7-hydroxy-2-(4-(methylthio)phenyl)-4H-chromen-4-one
75.8% inhibition at 0.1 mM
7-hydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
71.8% inhibition at 0.1 mM
7-hydroxy-2-(4-methoxyphenyl)-4H-chromen-4-one
75.2% inhibition at 0.1 mM
7-hydroxy-2-(5-methylfuran-2-yl)-4H-chromen-4-one
78.9% inhibition at 0.1 mM
7-hydroxy-2-(pyridin-2-yl)-4H-chromen-4-one
62.4% inhibition at 0.1 mM
7-hydroxy-2-(pyridin-3-yl)-4H-chromen-4-one
65.2% inhibition at 0.1 mM
7-hydroxy-2-(pyridin-4-yl)-4H-chromen-4-one
87.1% inhibition at 0.1 mM
8-hydroxyquinoline
time-dependent inactivation
Citric acid
inactivation at pH 5.5, Zn2+ protects
diethyl dicarbonate
-
rapid inactivation by modification of three essential His residues, at neutral pH, partial reactivation with hydroxylamine
ethyl-1H-tetrazole-4-acetate
-
0.14 mM, 9% inhibition
H-Gln-7-amido-4-methylcoumarin
imidazol-4-carbonic acid methylester
-
L-Gln-2-naphthylamide
substrate inhibition
L-glutamine-4-nitroanilide
substrate inhibition; substrate inhibition, isoDromeQC
L-glutaminyl-7-amido-4-methylcoumarin
-
substrate inhibition
L-glutaminyl-beta-naphthylamide
methyl N-[(2S)-1-hydroxy-2-[[3-(5-methyl-1H-imidazol-1-yl)propyl]amino]-3-phenylpropyl]-L-alaninate
-
N''-cyano-N-(2,3-dihydro-1,4-benzodioxin-6-yl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]guanidine
-
N''-cyano-N-(5-methyl-1H-imidazol-1-yl)-N'-(3,4,5-trimethoxyphenyl)guanidine
-
N''-cyano-N-methyl-N'-[3-(4-methyl-1H-imidazol-1-yl)propyl]guanidine
-
N''-cyano-N-methyl-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]guanidine
-
N,N-dimethylcysteamine
-
-
N-((E)-4-(3-(4-(2-aminoethyl)piperazin-1-yl)-3-oxoprop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-((E)-4-(3-oxo-3-(piperazin-1-yl)prop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-((E)-4-(3-oxo-3-(piperidin-4-ylamino)prop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-3,4-dimethoxy-benzenamine
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-(trifluoromethyl)-benzenamine
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-chlorobenzenamine
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-methoxybenzenamine
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)benzenamine
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)naphthalen-1-amine
-
N-(1-(3-(4-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-(trifluoromethyl)benzenamine
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-chloro-benzenamine
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)cyclohexanamine
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)naphthalen-1-amine
-
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
-
N-(3,4-dimethoxyphenyl)-4-[2-(5-methyl-1H-imidazol-1-yl)ethyl]-1,3-thiazol-2-amine
-
N-(3,4-dimethoxyphenyl)-5-[2-(5-methyl-1H-imidazol-1-yl)ethyl]-1,3,4-oxadiazol-2-amine
-
N-(3,4-dimethoxyphenyl)-N'-(4-methyl-1H-imidazol-1-yl)thiourea
-
N-(3,4-dimethoxyphenyl)-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N-(3,4-dimethoxyphenyl)-N'-1H-imidazol-1-ylthiourea
-
N-(3,4-dimethoxyphenyl)-N'-[3-(1H-imidazol-1-yl)-2-methylpropyl]thiourea
-
N-(3,4-dimethoxyphenyl)-N'-[3-(1H-imidazol-1-yl)propyl]thiourea
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
N-(3-(1H-imidazol-1-yl)propyl)-N-cyclohexyl-2-nitroethene-1,1-diamine
-
N-(3-(1H-imidazol-1-yl)propyl)-N-methyl-2-nitroethene-1,1-diamine
-
N-(3-(2-(2-aminopyridin-4-yl)ethoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-(2-aminoethoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-(3-(2-aminopyridin-4-yl)propoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-(3-aminopropoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-(4-(2-aminopyridin-4-yl)butoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-(4-(dimethylamino)butoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-(4-aminobutoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(3-methoxy-4-[[4-(piperidin-4-yl)phenyl]methoxy]phenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
-
N-(4'-fluoro[1,1'-biphenyl]-2-yl)-4-methyl-1H-imidazol-1-amine
-
N-(4-((1-(2-aminoethyl)piperidin-4-yl)carbamoyl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-(2-(((2-aminopyridin-4-yl)methyl)amino)-2-oxoethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-(2-((1-(2-aminoethyl)piperidin-4-yl)amino)-2-oxoethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-(2-(piperazin-1-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-(2-oxo-2-(piperazin-1-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-(2-oxo-2-(piperidin-4-ylamino)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-(4-(2-aminopyridin-4-yl)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-chlorophenyl)-N'-[2-(1H-imidazol-1-yl)propyl]-2-thioxoimidazolidin-4-one
-
N-(4-chlorophenyl)-N'-[3-(1H-imidazol-1-yl)propyl]thiourea
-
N-(4-methoxy-3-(2-(1-methylpiperidin-4-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(2-(piperazin-1-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(2-(piperidin-4-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(3-(methylamino)propoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(3-(piperazin-1-yl)propoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(3-(piperidin-4-yl)propoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(4-(methylamino)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(4-(piperazin-1-yl)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(4-(piperidin-4-yl)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-methoxy-3-(4-(pyrimidin-2-ylamino)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(4-[(1E)-3-[4-(2-aminoethyl)piperazin-1-yl]-3-oxoprop-1-en-1-yl]phenyl)-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N-(E)-(4-(3-(4-(2-aminoethyl)piperazin-1-yl)-3-oxoprop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
N-(trimethylsilyl)-imidazole
-
N-[3-(1H-imidazol-1-yl)propyl]-5-methoxy-1,3-benzothiazol-2-amine
-
-
N-[3-(1H-imidazol-1-yl)propyl]-6-methoxy-1,3-benzothiazol-2-amine
-
-
N-[3-(1H-imidazol-1-yl)propyl]-N'-phenylthiourea
-
N-[3-(4-aminobutoxy)-4-methoxyphenyl]-N'-[3-(2-methyl-1H-imidazol-1-yl)propyl]thiourea
-
N-[3-methoxy-4-[(piperidin-4-yl)methoxy]phenyl]-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N-[4-(2-aminoethoxy)-3-methoxyphenyl]-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N-[4-(3-aminopropoxy)-3-methoxyphenyl]-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N-[4-(4-aminobutoxy)-3-methoxyphenyl]-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N-[4-[3-(2-aminopyridin-4-yl)propoxy]-3-methoxyphenyl]-N'-(5-methyl-1H-imidazol-1-yl)thiourea
-
N2-[(2S)-1-hydroxy-2-[[3-(5-methyl-1H-imidazol-1-yl)propyl]amino]-3-phenylpropyl]-L-alaninamide
-
nitron
-
0.14 mM, 39% inhibition
oxalic acid diimidazolidide
-
PQ529
can efficiently inhibit the activity of both glutaminyl cyclase isozymes QC and isoQC. Treatment with PQ529 for 48 h significantly blocks the binding of CC2C6 to the cell surface in a dosage-dependent manner in wild-type, but not in isoQC-deficient cells
SEN-177
the triazole based inhibitor, SEN177 coordinates with the catalytically important Zn2+ ion of sQC and has made several hydrophobic interactions with active site residues such as W207, F325, and W329
1,10-phenanthroline
inactivated enzyme can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA, little reactivation by Co2+ and Mn2+
1,10-phenanthroline
time-dependent inactivation
1,10-phenanthroline
-
2 mM, complete inhibition
1,2-di-O-palmitoyl-3-O-(6'-deoxy-6'-sulfo-D-glycopyranosyl)-glycerol
-
1,2-di-O-palmitoyl-3-O-(6'-deoxy-6'-sulfo-D-glycopyranosyl)-glycerol
-
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
i.e. P150/03, complete inhibition at 0.01 mM
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
-
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
i.e. P150/03, complete inhibition at 0.01 mM
1-Benzylimidazole
isoDromeQC
1-Benzylimidazole
-
0.14 mM, 58% inhibition
1-Benzylimidazole
weak inhibition; weak inhibition
1-Methylimidazole
isoDromeQC
1-O-linolyl-2-O-palmitoyl-3-O-(6'-deoxy-6'-sulfo-D-glucopyranosyl)-glycerol
-
1-O-linolyl-2-O-palmitoyl-3-O-(6'-deoxy-6'-sulfo-D-glucopyranosyl)-glycerol
-
1-O-palmitoyl-2-O-linolenyl-3-O-(6'-deoxy-6'-sulfo-D-glucopyranosyl)-glycerol
-
1-O-palmitoyl-2-O-linolenyl-3-O-(6'-deoxy-6'-sulfo-D-glucopyranosyl)-glycerol
-
1-vinylimidazole
-
1-vinylimidazole
weak inhibition; weak inhibition
apigenin
75.2% inhibition at 0.1 mM
benzimidazole
-
-
benzimidazole
-
competitive
benzimidazole
-
competitive
benzylimidazole
-
benzylimidazole
-
competitive
benzylimidazole
-
competitive
cysteamine
isoDromeQC
dipicolinic acid
inactivated enzyme can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA, little reactivation by Co2+ and Mn2+
EFRH-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
EFRH-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
EFRHHDSGYE-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
EFRHHDSGYE-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
Gln-tert-butyl ester
-
-
H-Gln-7-amido-4-methylcoumarin
-
substrate inhibition
H-Gln-7-amido-4-methylcoumarin
-
substrate inhibition
H-Gln-7-amido-4-methylcoumarin
-
substrate inhibition
H-Gln-7-amido-4-methylcoumarin
substrate inhibition
H-Gln-beta-naphthylamide
-
substrate inhibition
H-Gln-beta-naphthylamide
-
substrate inhibition
H-Gln-beta-naphthylamide
-
substrate inhibition
H-Gln-beta-naphthylamide
substrate inhibition
imidazole
isoDromeQC
L-glutaminyl-beta-naphthylamide
-
substrate inhibition
L-glutaminyl-beta-naphthylamide
-
substrate inhibition
methylimidazole
-
-
N-(3,4-dimethoxyphenyl)-N'-[3-(1H-imidazol-1-yl)propyl]thiourea
-
N-(3,4-dimethoxyphenyl)-N'-[3-(1H-imidazol-1-yl)propyl]thiourea
-
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
-
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
-
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
-
N-diethylcysteamine
-
N-dimethylcysteamine
isoDromeQC
N-omega-acetylhistamine
isoDromeQC
N-omega-acetylhistamine
-
N-omega-acetylhistamine
-
-
N-omega-acetylhistamine
-
0.14 mM, 33% inhibition
N-omega-acetylhistamine
-
-
N-omega-acetylhistamine
weak inhibition; weak inhibition
Nomega-acetylhistamine
-
PBD150
potent competitive inhibitor, i.e. 1-(3,4-dimethoxyphenyl)-3-(3-imidazol-1-ylpropyl)thiourea; potent competitive inhibitor, i.e. 1-(3,4-dimethoxyphenyl)-3-(3-imidazol-1-ylpropyl)thiourea
PBD150
highly potent inhibitor
PBD150
highly potent inhibitor
PQ912
-
SEN177
i.e. 6''-fluoro-4-(4-methyl-4H-[1,2,4]triazol-3-yl)-3,4,5,6-tetrahydro-2H-[1,2',3',3'']terpyridine, binding structure with Golgi-resident hQC; i.e. 6''-fluoro-4-(4-methyl-4H-[1,2,4]triazol-3-yl)-3,4,5,6-tetrahydro-2H-[1,2',3',3'']terpyridine, binding structure with secretory hQC
additional information
phenol-40 (R1-), C5-OH (R2-) and C7-OH (R3-) modified apigenin derivatives are synthesized and evaluated as human QC (hQC) inhibitors, structure-function analysis, molecular docking, overview. No inhibition by 7-methoxy-2-(3-methylthiophen-2-yl)-4H-chromen-4-one, 7-methoxy-2-(4-methoxyphenyl)-4H-chromen-4-one, 7-methoxy-2-(2-methoxyphenyl)-4H-chromen-4-one, 2-(3,4-dimethoxyphenyl)-7-methoxy-4H-chromen-4-one, 7-methoxy-2-(3,4,5-trimethoxyphenyl)-4H-chromen-4-one, 2-(4-fluorophenyl)-7-methoxy-4H-chromen-4-one, 2-(3-fluorophenyl)-7-methoxy-4H-chromen-4-one, 7-methoxy-2-(2-(trifluoromethyl)phenyl)-4H-chromen-4-one, 7-methoxy-2-(pyridin-3-yl)-4H-chromen-4-one, 2-(furan-2-yl)-7-methoxy-4H-chromen-4-one, and 2-(furan-3-yl)-7-methoxy-4H-chromen-4-one
-
additional information
-
phenol-40 (R1-), C5-OH (R2-) and C7-OH (R3-) modified apigenin derivatives are synthesized and evaluated as human QC (hQC) inhibitors, structure-function analysis, molecular docking, overview. No inhibition by 7-methoxy-2-(3-methylthiophen-2-yl)-4H-chromen-4-one, 7-methoxy-2-(4-methoxyphenyl)-4H-chromen-4-one, 7-methoxy-2-(2-methoxyphenyl)-4H-chromen-4-one, 2-(3,4-dimethoxyphenyl)-7-methoxy-4H-chromen-4-one, 7-methoxy-2-(3,4,5-trimethoxyphenyl)-4H-chromen-4-one, 2-(4-fluorophenyl)-7-methoxy-4H-chromen-4-one, 2-(3-fluorophenyl)-7-methoxy-4H-chromen-4-one, 7-methoxy-2-(2-(trifluoromethyl)phenyl)-4H-chromen-4-one, 7-methoxy-2-(pyridin-3-yl)-4H-chromen-4-one, 2-(furan-2-yl)-7-methoxy-4H-chromen-4-one, and 2-(furan-3-yl)-7-methoxy-4H-chromen-4-one
-
additional information
structure-activity relationship analysis of Phe-Arg mimetic region of human glutaminyl cyclase inhibitors. Developed of QC inhibitors that contain 3-aminoalkyloxy-4-methoxyphenyl and 4-aminoalkyloxyphenyl groups to replace the previously developed pharmacophore, overview. In vivo activity of the compounds is analyzed using HT-22 cells, an immortalized hippocampal neuronal cell line
-
additional information
-
structure-activity relationship analysis of Phe-Arg mimetic region of human glutaminyl cyclase inhibitors. Developed of QC inhibitors that contain 3-aminoalkyloxy-4-methoxyphenyl and 4-aminoalkyloxyphenyl groups to replace the previously developed pharmacophore, overview. In vivo activity of the compounds is analyzed using HT-22 cells, an immortalized hippocampal neuronal cell line
-
additional information
development of small molecule inhibitors of glutaminyl cyclase and isoglutaminyl cyclase for Alzheimers disease, overview; development of small molecule inhibitors of glutaminyl cyclase and isoglutaminyl cyclase for Alzheimers disease, overview. Weak inhibition by imidazole derivatives
-
additional information
development of small molecule inhibitors of glutaminyl cyclase and isoglutaminyl cyclase for Alzheimers disease, overview; development of small molecule inhibitors of glutaminyl cyclase and isoglutaminyl cyclase for Alzheimers disease, overview. Weak inhibition by imidazole derivatives
-
additional information
crystal structures of weak binding inhibitors of human QC isozymes, all share the imidazole ring as the Zn(II) binding moiety, overview; crystal structures of weak binding inhibitors of human QC isozymes, share the imidazole ring as the Zn(II) binding moiety, overview
-
additional information
crystal structures of weak binding inhibitors of human QC isozymes, all share the imidazole ring as the Zn(II) binding moiety, overview; crystal structures of weak binding inhibitors of human QC isozymes, share the imidazole ring as the Zn(II) binding moiety, overview
-
additional information
-
crystal structures of weak binding inhibitors of human QC isozymes, all share the imidazole ring as the Zn(II) binding moiety, overview; crystal structures of weak binding inhibitors of human QC isozymes, share the imidazole ring as the Zn(II) binding moiety, overview
-
additional information
natural products from microalgae, such as Scenedesmus rubescens strain SAG 5.95, Scenedesmus producto-capitatus strain SAG 21.81, Scenedesmus accuminatus strain SAG 38.81, Scenedesmus pectinatus strain SAG 2003, Tetradesmus wisconsinensis strain SAG 3.99, and Eustigmatos magnus strain SAG 36.89, show potential against Alzheimers disease, sulfolipids are potent glutaminyl cyclase inhibitors. Mass spectrometric identification and analysis (high resolution ESI-FTIC-MS and UPLC-MS, UPLC/ESI-MSn measurements). The sulfolipids share common, necessary substructures with pharmacophore characteristics of known QC inhibitors
-
additional information
structure-function analysis of enzyme inhibitors, overview; structure-function analysis of enzyme inhibitors, overview. Natural products and their derivatives belonging to the sulfolipid family and isolated from methanol extracts of different algae species (such as Scenedesmus rubescens, Scenedesmus producto-capitatus, Scenedesmus accuminatus, Scenedesmus pectinatus, Tetradesmus wisconsinensis, and Eustigmatos magnusa) act as inhibitors of sQC. Synthesis and evaluation of benzimidazole based inhibitors, overview
-
additional information
structure-function analysis of enzyme inhibitors, overview; structure-function analysis of enzyme inhibitors, overview. Natural products and their derivatives belonging to the sulfolipid family and isolated from methanol extracts of different algae species (such as Scenedesmus rubescens, Scenedesmus producto-capitatus, Scenedesmus accuminatus, Scenedesmus pectinatus, Tetradesmus wisconsinensis, and Eustigmatos magnusa) act as inhibitors of sQC. Synthesis and evaluation of benzimidazole based inhibitors, overview
-
additional information
-
structure-function analysis of enzyme inhibitors, overview; structure-function analysis of enzyme inhibitors, overview. Natural products and their derivatives belonging to the sulfolipid family and isolated from methanol extracts of different algae species (such as Scenedesmus rubescens, Scenedesmus producto-capitatus, Scenedesmus accuminatus, Scenedesmus pectinatus, Tetradesmus wisconsinensis, and Eustigmatos magnusa) act as inhibitors of sQC. Synthesis and evaluation of benzimidazole based inhibitors, overview
-
additional information
in vitro and in silico determination of glutaminyl cyclase inhibitors, heterocyclic and peptidomimetic derivatives are synthesized and are able to inhibit the hQC enzyme, overview. The binding mechanism at the atomic level is estimated using molecular docking, free energy perturbation, and quantum chemical calculation methods. The predicted log(BBB) and human intestinal absorption values indicated that these compounds are able to permeate the blood-brain barrier and be well-absorbed through the gastrointestinal tract. Molecular docking study and atomistic molecular dynamics simulations, overview
-
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Alzheimer Disease
2D- and 3D-QSAR Modeling of Imidazole-Based Glutaminyl Cyclase Inhibitors.
Alzheimer Disease
An overview of glutaminyl cyclase inhibitors for Alzheimer's disease.
Alzheimer Disease
Discovery of highly potent human glutaminyl cyclase (QC) inhibitors as anti-Alzheimer's agents by the combination of pharmacophore-based and structure-based design.
Alzheimer Disease
Discovery of Potent Human Glutaminyl Cyclase Inhibitors as Anti-Alzheimer's Agents Based on Rational Design.
Alzheimer Disease
Distinct glutaminyl cyclase expression in Edinger-Westphal nucleus, locus coeruleus and nucleus basalis Meynert contributes to pGlu-Abeta pathology in Alzheimer's disease.
Alzheimer Disease
Disturbed ca(2+) homeostasis increases glutaminyl cyclase expression; connecting two early pathogenic events in Alzheimer's disease in vitro.
Alzheimer Disease
Exploring the binding mode of PQ912 against secretory glutaminyl cyclase through systematic exploitation of conformational ensembles.
Alzheimer Disease
Glutaminyl cyclase activity correlates with levels of A? peptides and mediators of angiogenesis in cerebrospinal fluid of Alzheimer's disease patients.
Alzheimer Disease
Glutaminyl cyclase in human cortex: correlation with (pGlu)-amyloid-? load and cognitive decline in Alzheimer's disease.
Alzheimer Disease
Glutaminyl cyclase inhibition attenuates pyroglutamate Abeta and Alzheimer's disease-like pathology.
Alzheimer Disease
Glutaminyl cyclase inhibitor contributes to the regulation of HSP70, HSP90, actin, and ribosome on gene and protein levels in vitro.
Alzheimer Disease
Glutaminyl cyclase inhibitor exhibits anti-inflammatory effects in both AD and LPS-induced inflammatory model mice.
Alzheimer Disease
Human glutaminyl cyclase: Structure, function, inhibitors and involvement in Alzheimer's disease.
Alzheimer Disease
Hydrazides Are Potent Transition-State Analogues for Glutaminyl Cyclase Implicated in the Pathogenesis of Alzheimer's Disease.
Alzheimer Disease
Hypothesis: glutaminyl cyclase inhibitors decrease risks of Alzheimer's disease and related dementias.
Alzheimer Disease
Identification of thyrotropin-releasing hormone as hippocampal glutaminyl cyclase substrate in neurons and reactive astrocytes.
Alzheimer Disease
Identifying hQC Inhibitors of Alzheimer's Disease by Effective Customized Pharmacophore-Based Virtual Screening, Molecular Dynamic Simulation, and Binding Free Energy Analysis.
Alzheimer Disease
In silico exploration of the fingerprints triggering modulation of glutaminyl cyclase inhibition for the treatment of Alzheimer's disease using SMILES based attributes in Monte Carlo optimization.
Alzheimer Disease
Increased glutaminyl cyclase activity in brains of Alzheimer's disease individuals.
Alzheimer Disease
Increased glutaminyl cyclase expression in peripheral blood of Alzheimer's disease patients.
Alzheimer Disease
Inhibition of glutaminyl cyclase ameliorates amyloid pathology in an animal model of Alzheimer's disease via the modulation of ?-secretase activity.
Alzheimer Disease
Inhibitors for Human Glutaminyl Cyclase by Structure Based Design and Bioisosteric Replacement.
Alzheimer Disease
Inhibitory effect of flavonoids on human glutaminyl cyclase.
Alzheimer Disease
Isoglutaminyl cyclase contributes to CCL2-driven neuroinflammation in Alzheimer's disease.
Alzheimer Disease
Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae.
Alzheimer Disease
Natural Products from Microalgae with Potential against Alzheimer's Disease: Sulfolipids Are Potent Glutaminyl Cyclase Inhibitors.
Alzheimer Disease
Potent human glutaminyl cyclase inhibitors as potential anti-Alzheimer's agents: Structure-activity relationship study of Arg-mimetic region.
Alzheimer Disease
PYROGLUTAMATE FORMATION AT THE N-TERMINI OF ABRI MOLECULES IN FAMILIAL BRITISH DEMENTIA IS NOT RESTRICTED TO THE CENTRAL NERVOUS SYSTEM.
Alzheimer Disease
Repurposing FDA-Approved Compounds for the Discovery of Glutaminyl Cyclase Inhibitors as Drugs Against Alzheimer's Disease.
Alzheimer Disease
Safety, tolerability and efficacy of the glutaminyl cyclase inhibitor PQ912 in Alzheimer's disease: results of a randomized, double-blind, placebo-controlled phase 2a study.
Alzheimer Disease
Structure-activity relationships of benzimidazole-based glutaminyl cyclase inhibitors featuring a heteroaryl scaffold.
Alzheimer Disease
Structures of Human Golgi-resident Glutaminyl Cyclase and Its Complexes with Inhibitors Reveal a Large Loop Movement upon Inhibitor Binding.
Alzheimer Disease
Synthesis and Evaluation of Diphenyl Conjugated Imidazole Derivatives as Potential Glutaminyl Cyclase Inhibitors for Treatment of Alzheimer's Disease.
Alzheimer Disease
Synthesis and evaluation of [(11)C]PBD150, a radiolabeled glutaminyl cyclase inhibitor for the potential detection of Alzheimer's disease prior to amyloid ? aggregation.
Alzheimer Disease
The soluble Y115E-Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease.
Alzheimer Disease
The structure of the human glutaminyl cyclase-SEN177 complex indicates routes for developing new potent inhibitors as possible agents for the treatment of neurological disorders.
Amyloidosis
Glutaminyl cyclase inhibition attenuates pyroglutamate Abeta and Alzheimer's disease-like pathology.
Amyloidosis
PYROGLUTAMATE FORMATION AT THE N-TERMINI OF ABRI MOLECULES IN FAMILIAL BRITISH DEMENTIA IS NOT RESTRICTED TO THE CENTRAL NERVOUS SYSTEM.
Anemia
Luteolin promotes macrophage-mediated phagocytosis by inhibiting CD47 pyroglutamation.
Arthritis, Rheumatoid
Expression of human and Porphyromonas gingivalis glutaminyl cyclases in periodontitis and rheumatoid arthritis-A pilot study.
Brain Ischemia
Alterations in mRNA expression of BACE1, cathepsin B, and glutaminyl cyclase in mice ischemic brain.
Chronic Periodontitis
Expression of human and Porphyromonas gingivalis glutaminyl cyclases in periodontitis and rheumatoid arthritis-A pilot study.
Dementia
Glutaminyl cyclase inhibition attenuates pyroglutamate Abeta and Alzheimer's disease-like pathology.
Dementia
Hypothesis: glutaminyl cyclase inhibitors decrease risks of Alzheimer's disease and related dementias.
Dementia
Increased glutaminyl cyclase expression in peripheral blood of Alzheimer's disease patients.
Goiter
Role of glutaminyl cyclases in thyroid carcinomas.
Hypogonadism
Glutaminyl cyclase (QC) knock out mice show mild hypothyreodism but absence of hypogonadism: implications for enzyme function and drug development.
Insulinoma
Isolation, catalytic properties, and competitive inhibitors of the zinc-dependent murine glutaminyl cyclase.
Melanoma
Microarray evidence of glutaminyl cyclase gene expression in melanoma: implications for tumor antigen specific immunotherapy.
Neoplasms
Enhancement of epidermal growth factor receptor antibody tumor immunotherapy by glutaminyl cyclase inhibition to interfere with CD47/signal regulatory protein alpha interactions.
Neoplasms
Glutaminyl cyclase is an enzymatic modifier of the CD47- SIRP? axis and a target for cancer immunotherapy.
Neoplasms
Microarray evidence of glutaminyl cyclase gene expression in melanoma: implications for tumor antigen specific immunotherapy.
Neoplasms
Proteomic Characterization of Two Medically Important Malaysian Snake Venoms, Calloselasma rhodostoma (Malayan Pit Viper) and Ophiophagus hannah (King Cobra).
Neurodegenerative Diseases
2D- and 3D-QSAR Modeling of Imidazole-Based Glutaminyl Cyclase Inhibitors.
Neurodegenerative Diseases
The soluble Y115E-Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease.
Neuroinflammatory Diseases
Isoglutaminyl cyclase contributes to CCL2-driven neuroinflammation in Alzheimer's disease.
Obesity
A nonsense loss-of-function mutation in PCSK1 contributes to dominantly inherited human obesity.
Obesity
What model organisms and interactomics can reveal about the genetics of human obesity.
Overweight
Replication of Established Common Genetic Variants for Adult BMI and Childhood Obesity in Greek Adolescents: The TEENAGE Study.
Pediatric Obesity
Role of BMI-Associated Loci Identified in GWAS Meta-Analyses in the Context of Common Childhood Obesity in European Americans.
Periodontitis
Expression of human and Porphyromonas gingivalis glutaminyl cyclases in periodontitis and rheumatoid arthritis-A pilot study.
Pheochromocytoma
Identification of potential gene markers and insights into the pathophysiology of pheochromocytoma malignancy.
Synucleinopathies
A glutaminyl cyclase-catalyzed ?-synuclein modification identified in human synucleinopathies.
Thyroid Neoplasms
Role of glutaminyl cyclases in thyroid carcinomas.
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1.24
2-amino-5-(butan-2-ylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.32
2-amino-5-(cyclohexylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.22
2-amino-5-(cyclopropylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.69
2-amino-5-oxo-5-(propan-2-ylamino)pentanoic acid
-
pH and temperature not specified in the publication
0.44
2-amino-5-oxo-5-[(2-phenylethyl)amino]pentanoic acid
-
pH and temperature not specified in the publication
0.38
2-amino-5-[(2-methylbutyl)amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
1.62
2-amino-5-[(2S)-butan-2-ylamino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.38
2-amino-5-[[(2S)-2-methylbutyl]amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
6
EFRH-NH2
-
at pH 6.5, 10times higher compared to KM-value of Gln substrate
0.042
Gln 7-amido-4-methylcoumarin
-
pH 8.0, 30°C
0.087 - 0.155
Gln(3)-amyloid-beta peptide 3-11 amide
-
0.162
Gln(3)-amyloid-beta peptide 3-21 amide
-
pH 6.0, 30°C, 1% DMSO
-
0.089
Gln(3)-amyloid-beta peptide 3-40 amide
-
pH 6.0, 30°C, 1% DMSO
-
0.058 - 1.1
Gln-2-naphthylamide
0.054
Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
0.065 - 0.197
Gln-Ala-Ala-Ala-Ala-NH2
0.087 - 0.164
Gln-Ala-Ala-NH2
0.079 - 0.216
Gln-Ala-Ala-Ser-Ala-Ala-NH2
0.065 - 0.143
Gln-Arg-Gly-Ile-NH2
0.055 - 0.124
Gln-Arg-Tyr-Phe-NH2
0.153 - 0.172
Gln-Asn-Gly-Ile-NH2
0.07
Gln-beta-naphthylamide
-
pH 8.0, 30°C
0.038
Gln-beta-naphthylamine
-
pH 8.0, 30°C
0.148
Gln-Gln-OH
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.041 - 0.045
Gln-Gln-Tyr-Phe-NH2
0.077 - 0.102
Gln-Glu-Ala-Ala-NH2
0.039 - 0.081
Gln-Glu-Ala-Phe-NH2
0.055 - 0.107
Gln-Glu-Asp-Leu-NH2
0.069 - 0.113
Gln-Glu-Tyr-Ala-NH2
0.079 - 0.103
Gln-Glu-Tyr-NH2
0.047 - 0.1
Gln-Glu-Tyr-Phe-NH2
0.102 - 0.333
Gln-Gly-Pro
0.09
Gln-His-Pro-NH2
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.068 - 0.092
Gln-His-Tyr-Phe-NH2
0.034 - 0.118
Gln-Lys-Arg-Leu-NH2
0.069 - 0.111
Gln-Phe-Ala-NH2
0.149 - 18.89
Gln-Pro-Tyr-Phe-NH2
0.055 - 0.135
Gln-Ser-Tyr-Phe-NH2
0.223 - 6.7
Gln-tert-butyl ester
0.05 - 0.078
Gln-Trp-Ala-NH2
0.211
Gln-Tyr
-
pH 8.0, 30°C
0.058 - 0.101
Gln-Tyr-Ala
0.101 - 0.153
Gln-Tyr-Ala-OH
0.019
glucagon(3-29)
-
pH 6.0, 30°C, 1% DMSO
-
0.32
glutamine tert-butyl ester
-
-
0.063
gonadotropin releasing hormone
-
-
0.017 - 0.105
H-Gln-7-amido-4-methylcoumarin
0.487 - 2.3
H-Gln-Asp-Glu-Leu-NH2
0.028 - 0.17
H-Gln-beta-naphthylamide
0.08 - 0.742
H-Gln-Glu-Ala-Phe-NH2
0.265 - 29.5
H-Gln-Glu-OH
0.33
H-Gln-Glu-Tyr-Ala-NH2
pH 8.0, 30°C
0.065 - 0.41
H-Gln-Glu-Tyr-Phe-NH2
0.214 - 4.1
H-Gln-Gly-Pro-OH
0.06 - 0.448
H-Gln-Lys-Arg-Leu-NH2
0.106 - 0.44
H-Gln-Phe-Ala-NH2
0.128 - 0.35
H-Gln-Phe-Ala-OH
0.247
H-Gln-Ser-Tyr-Phe-NH2
pH 8.0, 30°C
0.72
H-Gln-Tyr-Ala-OH
30°C, isoDromeQC
0.014 - 0.282
H-Gln-Val-Ala-OH
0.14
L-gamma-glutamyl-(+)-3-aminobutyric acid
-
pH and temperature not specified in the publication
0.33
L-gamma-glutamyl-(+)-3-aminoisobutyric acid
-
pH and temperature not specified in the publication
0.91
L-gamma-glutamyl-beta-alanine
-
pH and temperature not specified in the publication
0.36
L-gamma-glutamyl-ethylamine
-
pH and temperature not specified in the publication
0.25
L-gamma-glutamyl-n-butylamine
-
pH and temperature not specified in the publication
0.32
L-gamma-glutamyl-n-propylamine
-
pH and temperature not specified in the publication
0.1
L-gamma-glutamylaniline
-
pH and temperature not specified in the publication
0.56
L-gamma-glutamylbenzylamine
-
pH and temperature not specified in the publication
0.084
L-gamma-glutamylcyclopentylamine
-
pH and temperature not specified in the publication
1.9
L-gamma-glutamylglycine
-
pH and temperature not specified in the publication
0.12
L-gamma-glutamylneohexylamine
-
pH and temperature not specified in the publication
0.61
L-gamma-glutamylneopentylamine
-
pH and temperature not specified in the publication
0.028 - 0.5
L-Gln-2-naphthylamide
0.048 - 0.3
L-Gln-7-amido-4-methylcoumarin
0.17 - 1.791
L-Gln-Gly-L-Pro
0.294 - 1.838
L-Gln-L-Ala
0.32
L-Gln-L-Arg-Gly-L-Ile-NH2
pH 8.0, 30°C
0.36
L-Gln-L-Asn-Gly-L-Ile-NH2
pH 8.0, 30°C
0.487 - 1.74
L-Gln-L-Asp-L-Glu-L-Leu-NH2
0.08 - 0.742
L-Gln-L-Glu-L-Ala-L-Phe-NH2
0.33
L-Gln-L-Glu-L-Tyr-L-Ala-NH2
pH 8.0, 30°C
0.086 - 0.41
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
0.06 - 0.448
L-Gln-L-Lys-L-Arg-L-Leu-NH2
0.106 - 0.44
L-Gln-L-Phe-L-Ala-NH2
0.247
L-Gln-L-Ser-L-Tyr-L-Phe-NH2
pH 8.0, 30°C
0.16
L-Gln-L-Thr-Gly-L-Ile-NH2
pH 8.0, 30°C
0.132
L-Gln-L-Thr-L-Ala
-
-
-
0.072
L-Gln-L-Trp-L-Ala-NH2
pH 8.0, 30°C
0.014 - 0.272
L-Gln-L-Val-L-Ala-NH2
0.151 - 8.2
L-Gln-tert-butyl ester
0.379 - 1.3
L-glutamine tert-butyl ester
0.0218
L-glutaminyl 2-naphthylamide
at pH 8.0 and 25°C
0.06
L-glutaminyl-2-naphthylamide
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.051
L-glutaminyl-4-methylcoumarinylamide
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.03 - 0.31
L-glutaminyl-7-amido-4-methylcoumarin
0.032 - 0.035
L-glutaminyl-beta-naphthylamide
0.032 - 0.063
N1-naphthalen-2-yl-L-glutamamide
0.27
Nepsilon-(L-gamma-glutamyl)-D-lysine
-
pH and temperature not specified in the publication
0.26
Nepsilon-(L-gamma-glutamyl)-L-lysine
-
pH and temperature not specified in the publication
20
O-(n-butylcarbamyl)-L-serine
-
pH and temperature not specified in the publication
0.4
QAAR
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.19
S-(cyclohexylamine)-L-cysteine
-
pH and temperature not specified in the publication
0.091
S-(n-butylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
0.093
S-(n-propylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
0.088
[Gln1,Gly4]-thyrotropin releasing hormone
-
-
-
0.087 - 0.151
[Gln1]-fertilization promoting peptide
-
0.031 - 0.033
[Gln1]-gastrin
-
0.053 - 0.054
[Gln1]-gonadotropin releasing-hormone
-
0.023 - 0.037
[Gln1]-neurotensin
0.09
[Gln1]-thyrotropin releasing-hormone
-
pH 8.0, 30°C
-
additional information
additional information
-
0.087
Gln(3)-amyloid-beta peptide 3-11 amide
-
pH 6.0, 30°C, in absence of DMSO
-
0.155
Gln(3)-amyloid-beta peptide 3-11 amide
-
pH 6.0, 30°C, 1% DMSO
-
0.058
Gln-2-naphthylamide
-
pH 8.0, 25°C, wild-type enzyme
0.125
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D248A
0.161
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme H319L
0.174
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme S160A
0.254
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D305N
0.33
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D248Q
0.431
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D305E
0.615
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme S160G
0.736
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme E201D
1.1
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D305A
0.143
Gln-Ala
-
pH 8.0, 30°C, 0.5 M KCl
0.158
Gln-Ala
-
pH 8.0, 30°C
0.232
Gln-Ala
-
pH 8.0, 30°C
0.357
Gln-Ala
-
pH 8.0, 30°C, 0.5 M KCl
0.065
Gln-Ala-Ala-Ala-Ala-NH2
-
pH 8.0, 30°C
0.197
Gln-Ala-Ala-Ala-Ala-NH2
-
pH 8.0, 30°C
0.087
Gln-Ala-Ala-NH2
-
pH 8.0, 30°Cl
0.164
Gln-Ala-Ala-NH2
-
pH 8.0, 30°Cl
0.079
Gln-Ala-Ala-Ser-Ala-Ala-NH2
-
pH 8.0, 30°C
0.216
Gln-Ala-Ala-Ser-Ala-Ala-NH2
-
pH 8.0, 30°C
0.065
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.091
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.123
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C
0.143
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C
0.055
Gln-Arg-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.124
Gln-Arg-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.153
Gln-Asn-Gly-Ile-NH2
-
pH 8.0, 30°C
0.172
Gln-Asn-Gly-Ile-NH2
-
pH 8.0, 30°C
0.044
Gln-Gln
-
pH 8.0, 30°C
0.092
Gln-Gln
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.11
Gln-Gln
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.148
Gln-Gln
-
pH 8.0, 30°C
0.59
Gln-Gln
pH 8.0, mutant enzyme W207F
0.63
Gln-Gln
pH 8.0, wild-type enzyme
0.76
Gln-Gln
pH 8.0, mutant enzyme R54W
0.79
Gln-Gln
pH 7.0, wild-type enzyme
0.82
Gln-Gln
pH 8.0, mutant enzyme F146A
0.9
Gln-Gln
pH 7.5, wild-type enzyme
0.9
Gln-Gln
pH 8.5, wild-type enzyme
1.16
Gln-Gln
pH 8.0, mutant enzyme Q304L
1.47
Gln-Gln
pH 8.0, mutant enzyme K144A
1.77
Gln-Gln
pH 8.0, mutant enzyme W207L
2.06
Gln-Gln
pH 8.8, wild-type enzyme
4.67
Gln-Gln
pH 8.0, mutant enzyme F325A
12.62
Gln-Gln
pH 8.0, mutant enzyme E201D
29.53
Gln-Gln
pH 8.0, mutant enzyme W329A
0.31
Gln-Gln-Gln
-
-
0.041
Gln-Gln-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.045
Gln-Gln-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.094
Gln-Glu
-
pH 8.0, 30°C, 0.5 M KCl
0.106
Gln-Glu
-
pH 8.0, 30°C
0.359
Gln-Glu
-
pH 8.0, 30°C
0.47
Gln-Glu
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.607
Gln-Glu
-
pH 8.0, 30°C, 0.5 M KCl
0.61
Gln-Glu
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.077
Gln-Glu-Ala-Ala-NH2
-
pH 8.0, 30°C
0.102
Gln-Glu-Ala-Ala-NH2
-
pH 8.0, 30°C
0.039
Gln-Glu-Ala-Phe-NH2
-
pH 8.0, 30°C
0.081
Gln-Glu-Ala-Phe-NH2
-
pH 8.0, 30°C
0.055
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C
0.061
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.094
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.107
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C
0.069
Gln-Glu-Tyr-Ala-NH2
-
pH 8.0, 30°C
0.113
Gln-Glu-Tyr-Ala-NH2
-
pH 8.0, 30°C
0.079
Gln-Glu-Tyr-NH2
-
pH 8.0, 30°C
0.103
Gln-Glu-Tyr-NH2
-
pH 8.0, 30°C
0.047
Gln-Glu-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.1
Gln-Glu-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.16
Gln-Gly
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.247
Gln-Gly
-
pH 8.0, 30°C
0.36
Gln-Gly
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.641
Gln-Gly
-
pH 8.0, 30°C
0.102
Gln-Gly-Pro
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.13
Gln-Gly-Pro
-
pH 8.0, 30°C
0.23
Gln-Gly-Pro
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.333
Gln-Gly-Pro
-
pH 8.0, 30°C
0.068
Gln-His-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.092
Gln-His-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.034
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.053
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.054
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C
0.118
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C
0.401
Gln-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.409
Gln-NH2
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.409
Gln-NH2
-
pH 8.0, 30°C
0.433
Gln-NH2
-
pH 8.0, 30°C
0.446
Gln-NH2
-
pH 8.0, 30°C, 0.5 M KCl
1.1
Gln-NH2
-
wild-type enzyme
4.3
Gln-NH2
-
mutant enzyme H307Q
4.9
Gln-NH2
-
mutant enzyme H319Q
0.06
Gln-Phe-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.1
Gln-Phe-Ala
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.069
Gln-Phe-Ala-NH2
-
pH 8.0, 30°C
0.111
Gln-Phe-Ala-NH2
-
pH 8.0, 30°C
0.149
Gln-Pro-Tyr-Phe-NH2
-
pH 8.0, 30°C
18.89
Gln-Pro-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.055
Gln-Ser-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.135
Gln-Ser-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.223
Gln-tert-butyl ester
-
pH 8.0, 30°C
1.235
Gln-tert-butyl ester
-
pH 8.0, 30°C
4.1
Gln-tert-butyl ester
-
-
6.7
Gln-tert-butyl ester
-
-
0.05
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C
0.056
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.072
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.078
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C
0.058
Gln-Tyr-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.063
Gln-Tyr-Ala
-
pH 8.0, 30°C
0.08
Gln-Tyr-Ala
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.101
Gln-Tyr-Ala
-
pH 8.0, 30°C
0.101
Gln-Tyr-Ala-OH
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.153
Gln-Tyr-Ala-OH
-
37°C, recombinant enzyme, expressed in Pichia pastoris
0.12
Gln-Val
-
-
0.196
Gln-Val
-
pH 8.0, 30°C
0.017
H-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
0.08
H-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
0.105
H-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
0.294
H-Gln-Ala-OH
-
pH 8.0, 30°C
1.838
H-Gln-Ala-OH
pH 8.0, 30°C
2.8
H-Gln-Ala-OH
30°C, isoDromeQC
0.487
H-Gln-Asp-Glu-Leu-NH2
-
pH 8.0, 30°C
1.748
H-Gln-Asp-Glu-Leu-NH2
pH 8.0, 30°C
2.3
H-Gln-Asp-Glu-Leu-NH2
30°C
0.028
H-Gln-beta-naphthylamide
-
pH 8.0, 30°C
0.036
H-Gln-beta-naphthylamide
-
pH 8.0, 30°C
0.056
H-Gln-beta-naphthylamide
pH 8.0, 30°C
0.15
H-Gln-beta-naphthylamide
30°C, isoDromeQC
0.17
H-Gln-beta-naphthylamide
30°C
0.053
H-Gln-Gln-OH
-
pH 8.0, 30°C
0.115
H-Gln-Gln-OH
-
pH 8.0, 30°C
0.487
H-Gln-Gln-OH
pH 8.0, 30°C
0.94
H-Gln-Gln-OH
30°C, isoDromeQC
0.08
H-Gln-Glu-Ala-Phe-NH2
-
pH 8.0, 30°C
0.42
H-Gln-Glu-Ala-Phe-NH2
30°C
0.68
H-Gln-Glu-Ala-Phe-NH2
30°C, isoDromeQC
0.742
H-Gln-Glu-Ala-Phe-NH2
pH 8.0, 30°C
0.265
H-Gln-Glu-OH
-
pH 8.0, 30°C
0.705
H-Gln-Glu-OH
-
pH 8.0, 30°C
2.516
H-Gln-Glu-OH
pH 8.0, 30°C
0.065
H-Gln-Glu-Tyr-Phe-NH2
30°C
0.086
H-Gln-Glu-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.41
H-Gln-Glu-Tyr-Phe-NH2
pH 8.0, 30°C
0.424
H-Gln-Gly-OH
-
pH 8.0, 30°C
1.1
H-Gln-Gly-OH
-
pH 8.0, 30°C
2.4
H-Gln-Gly-OH
30°C, isoDromeQC
2.64
H-Gln-Gly-OH
pH 8.0, 30°C
0.214
H-Gln-Gly-Pro-OH
-
pH 8.0, 30°C
0.59 - 1
H-Gln-Gly-Pro-OH
-
pH 8.0, 30°C
1.17
H-Gln-Gly-Pro-OH
30°C, isoDromeQC
1.791
H-Gln-Gly-Pro-OH
pH 8.0, 30°C
4.1
H-Gln-Gly-Pro-OH
30°C
0.06
H-Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C
0.08
H-Gln-Lys-Arg-Leu-NH2
30°C
0.448
H-Gln-Lys-Arg-Leu-NH2
pH 8.0, 30°C
0.48
H-Gln-NH2
-
pH 8.0, 30°C
2.048
H-Gln-NH2
pH 8.0, 30°C
0.106
H-Gln-Phe-Ala-NH2
-
pH 8.0, 30°C
0.44
H-Gln-Phe-Ala-NH2
pH 8.0, 30°C
0.128
H-Gln-Phe-Ala-OH
30°C, isoDromeQC
0.35
H-Gln-Phe-Ala-OH
30°C
0.014
H-Gln-Val-Ala-OH
-
pH 8.0, 30°C
0.1293
H-Gln-Val-Ala-OH
30°C, isoDromeQC
0.14
H-Gln-Val-Ala-OH
30°C
0.282
H-Gln-Val-Ala-OH
pH 8.0, 30°C
0.028
L-Gln-2-naphthylamide
-
pH 8.0, 30°C
0.039
L-Gln-2-naphthylamide
mutant enzyme E45Q, at pH 7.0 at 25°C
0.04
L-Gln-2-naphthylamide
pH 8.0, 30°C
0.056
L-Gln-2-naphthylamide
pH 8.0, 30°C
0.121
L-Gln-2-naphthylamide
wild type enzyme, at pH 7.0 at 25°C
0.4
L-Gln-2-naphthylamide
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.5
L-Gln-2-naphthylamide
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.048
L-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
0.05
L-Gln-7-amido-4-methylcoumarin
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.08
L-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
0.105
L-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
0.3
L-Gln-7-amido-4-methylcoumarin
in 0.1 M MES, pH 6.0, temperature not specified in the publication
2.7
L-Gln-amide
in 0.1 M MES, pH 7.5, temperature not specified in the publication
2.9
L-Gln-amide
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.41
L-Gln-Gly
pH 8.0, 30°C
1.1
L-Gln-Gly
-
pH 8.0, 30°C
2.64
L-Gln-Gly
pH 8.0, 30°C
3.8
L-Gln-Gly
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.17
L-Gln-Gly-L-Pro
pH 8.0, 30°C
0.59 - 1
L-Gln-Gly-L-Pro
-
pH 8.0, 30°C
1.791
L-Gln-Gly-L-Pro
pH 8.0, 30°C
0.294
L-Gln-L-Ala
-
pH 8.0, 30°C
0.4
L-Gln-L-Ala
pH 8.0, 30°C
1.838
L-Gln-L-Ala
pH 8.0, 30°C
0.487
L-Gln-L-Asp-L-Glu-L-Leu-NH2
-
pH 8.0, 30°C
1.74
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pH 8.0, 30°C
0.053
L-Gln-L-Gln
-
pH 8.0, 30°C
0.15
L-Gln-L-Gln
pH 8.0, 30°C
0.487
L-Gln-L-Gln
pH 8.0, 30°C
6.5
L-Gln-L-Gln
in 0.1 M MES, pH 7.5, temperature not specified in the publication
20.4
L-Gln-L-Gln
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.265
L-Gln-L-Glu
-
pH 8.0, 30°C
0.8
L-Gln-L-Glu
pH 8.0, 30°C
2.4
L-Gln-L-Glu
in 0.1 M MES, pH 7.5, temperature not specified in the publication
2.516
L-Gln-L-Glu
pH 8.0, 30°C
4.2
L-Gln-L-Glu
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.08
L-Gln-L-Glu-L-Ala-L-Phe-NH2
-
pH 8.0, 30°C
0.742
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pH 8.0, 30°C
0.086
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
-
pH 8.0, 30°C
0.41
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pH 8.0, 30°C
0.06
L-Gln-L-Lys-L-Arg-L-Leu-NH2
-
pH 8.0, 30°C
0.448
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pH 8.0, 30°C
0.106
L-Gln-L-Phe-L-Ala-NH2
-
pH 8.0, 30°C
0.44
L-Gln-L-Phe-L-Ala-NH2
pH 8.0, 30°C
0.014
L-Gln-L-Val-L-Ala-NH2
-
pH 8.0, 30°C
0.272
L-Gln-L-Val-L-Ala-NH2
pH 8.0, 30°C
0.48
L-Gln-NH2
-
pH 8.0, 30°C
2.048
L-Gln-NH2
pH 8.0, 30°C
0.151
L-Gln-tert-butyl ester
-
pH 8.0, 30°C
0.294
L-Gln-tert-butyl ester
pH 8.0, 30°C
1
L-Gln-tert-butyl ester
in 0.1 M MES, pH 7.5, temperature not specified in the publication
8.2
L-Gln-tert-butyl ester
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.379
L-glutamine tert-butyl ester
-
pH 6.5
0.4
L-glutamine tert-butyl ester
-
pH 6.75
0.43
L-glutamine tert-butyl ester
-
pH 7.45
0.44
L-glutamine tert-butyl ester
-
pH 8.05
0.46
L-glutamine tert-butyl ester
-
pH 7.0 or pH 8.6
0.55
L-glutamine tert-butyl ester
-
pH 6.2
0.6
L-glutamine tert-butyl ester
-
pH 9.0
0.62
L-glutamine tert-butyl ester
-
pH 6.3
0.9
L-glutamine tert-butyl ester
-
pH 9.55
1.3
L-glutamine tert-butyl ester
-
pH 9.95
0.03
L-glutaminyl-7-amido-4-methylcoumarin
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.03
L-glutaminyl-7-amido-4-methylcoumarin
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.205
L-glutaminyl-7-amido-4-methylcoumarin
30°C, isoDromeQC
0.31
L-glutaminyl-7-amido-4-methylcoumarin
30°C
0.032
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.035
L-glutaminyl-beta-naphthylamide
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.032
N1-naphthalen-2-yl-L-glutamamide
-
pH 8.0, 30°C, 0.5 M KCl
0.063
N1-naphthalen-2-yl-L-glutamamide
-
pH 8.0, 30°C, 0.5 M KCl
1.1
QAAE
in 0.1 M MES, pH 7.5, temperature not specified in the publication
1.6
QAAE
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.1
QAAF
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.8
QAAF
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.2
QAEA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.7
QAEA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
2.1
QAFA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
2.5
QAFA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.1
QARA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
24.4
QARA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
1
QEAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
1.1
QEAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.16
QEDL
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.16
QEDL
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.029
QEYF
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.04
QEYF
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
1.9
QFAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
3.5
QFAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.1
QGGG
in 0.1 M MES, pH 7.5, temperature not specified in the publication
5.6
QGGG
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.9
QRAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
2.9
QRAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.087
[Gln1]-fertilization promoting peptide
-
pH 8.0, 30°C
-
0.151
[Gln1]-fertilization promoting peptide
-
pH 8.0, 30°C
-
0.031
[Gln1]-gastrin
-
pH 8.0, 30°C
-
0.033
[Gln1]-gastrin
-
pH 8.0, 30°C
-
0.053
[Gln1]-gonadotropin releasing-hormone
-
pH 8.0, 30°C
-
0.054
[Gln1]-gonadotropin releasing-hormone
-
pH 8.0, 30°C
-
0.023
[Gln1]-neurotensin
-
pH 8.0, 30°C
0.037
[Gln1]-neurotensin
-
pH 8.0, 30°C
additional information
additional information
-
-
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.07
2-amino-5-(butan-2-ylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.061
2-amino-5-(cyclohexylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.045
2-amino-5-(cyclopropylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.068
2-amino-5-oxo-5-(propan-2-ylamino)pentanoic acid
-
pH and temperature not specified in the publication
0.17
2-amino-5-oxo-5-[(2-phenylethyl)amino]pentanoic acid
-
pH and temperature not specified in the publication
0.19
2-amino-5-[(2-methylbutyl)amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.11
2-amino-5-[(2S)-butan-2-ylamino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.21
2-amino-5-[[(2S)-2-methylbutyl]amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.00022
EFRH-NH2
-
at pH 6.5, 150000fold lower compared to Gln substrate
0.00042
EFRHHDSGYE-NH2
-
-
39.4
Gln 7-amido-4-methylcoumarin
-
pH 8.0, 30°C
41.4 - 55
Gln(3)-amyloid-beta peptide 3-11 amide
-
62
Gln(3)-amyloid-beta peptide 3-21 amide
-
pH 6.0, 30°C, 1% DMSO
-
40
Gln(3)-amyloid-beta peptide 3-40 amide
-
pH 6.0, 30°C, 1% DMSO
-
0.0019 - 5.4
Gln-2-naphthylamide
5.3
Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
60.5 - 74.6
Gln-Ala-Ala-Ala-Ala-NH2
76.3 - 83.2
Gln-Ala-Ala-NH2
55.3 - 78.5
Gln-Ala-Ala-Ser-Ala-Ala-NH2
29.8 - 49.2
Gln-Arg-Gly-Ile-NH2
29.6 - 48.9
Gln-Arg-Tyr-Phe-NH2
51.4 - 56.6
Gln-Asn-Gly-Ile-NH2
20.6
Gln-beta-naphthylamide
-
pH 8.0, 30°C
51.4
Gln-beta-naphthylamine
-
pH 8.0, 30°C
12.8
Gln-Gln-OH
-
30°C, recombinant enzyme, expressed in Pichia pastoris
41.4 - 52.9
Gln-Gln-Tyr-Phe-NH2
46 - 53.7
Gln-Glu-Ala-Ala-NH2
39 - 48.5
Gln-Glu-Ala-Phe-NH2
45.6 - 58.5
Gln-Glu-Asp-Leu-NH2
42.1 - 44.7
Gln-Glu-Tyr-Ala-NH2
45.1 - 53.6
Gln-Glu-Tyr-NH2
46 - 54.6
Gln-Glu-Tyr-Phe-NH2
83
Gln-His-Pro-NH2
-
30°C, recombinant enzyme, expressed in Pichia pastoris
55.4 - 75.9
Gln-His-Tyr-Phe-NH2
31.6 - 58.1
Gln-Lys-Arg-Leu-NH2
109 - 132
Gln-Phe-Ala-NH2
18.8 - 31.7
Gln-Pro-Tyr-Phe-NH2
52.8 - 64.9
Gln-Ser-Tyr-Phe-NH2
6.7 - 49.4
Gln-tert-butyl ester
47 - 151.8
Gln-Trp-Ala-NH2
94
Gln-Tyr
-
pH 8.0, 30°C
17.2
Gln-Val
-
pH 8.0, 30°C
10
glucagon(3-29)
-
pH 6.0, 30°C, 1% DMSO
-
1.07 - 25
H-Gln-7-amido-4-methylcoumarin
13.1 - 40
H-Gln-Asp-Glu-Leu-NH2
1.1 - 45
H-Gln-beta-naphthylamide
11 - 64
H-Gln-Glu-Ala-Phe-NH2
49
H-Gln-Glu-Tyr-Ala-NH2
pH 8.0, 30°C
6.9 - 50
H-Gln-Glu-Tyr-Phe-NH2
4.02 - 32
H-Gln-Gly-Pro-OH
7 - 62
H-Gln-Lys-Arg-Leu-NH2
55 - 57
H-Gln-Phe-Ala-NH2
44
H-Gln-Ser-Tyr-Phe-NH2
pH 8.0, 30°C
17.04
H-Gln-Tyr-Ala-OH
30°C, isoDromeQC
3.02 - 27
H-Gln-Val-Ala-OH
0.054
L-gamma-glutamyl-(+)-3-aminobutyric acid
-
pH and temperature not specified in the publication
0.21
L-gamma-glutamyl-(+)-3-aminoisobutyric acid
-
pH and temperature not specified in the publication
0.18
L-gamma-glutamyl-beta-alanine
-
pH and temperature not specified in the publication
0.038
L-gamma-glutamyl-ethylamine
-
pH and temperature not specified in the publication
0.02
L-gamma-glutamyl-methylamine
-
pH and temperature not specified in the publication
0.21
L-gamma-glutamyl-n-butylamine
-
pH and temperature not specified in the publication
0.23
L-gamma-glutamyl-n-propylamine
-
pH and temperature not specified in the publication
0.012
L-gamma-glutamyl-tert-butylamine
-
kcat less than 0.012 s-1, pH and temperature not specified in the publication
0.036
L-gamma-glutamylaniline
-
pH and temperature not specified in the publication
0.4
L-gamma-glutamylbenzylamine
-
pH and temperature not specified in the publication
0.076
L-gamma-glutamylcyclopentylamine
-
pH and temperature not specified in the publication
0.14
L-gamma-glutamylglycine
-
pH and temperature not specified in the publication
0.18
L-gamma-glutamylneohexylamine
-
pH and temperature not specified in the publication
0.035
L-gamma-glutamylneopentylamine
-
pH and temperature not specified in the publication
1.4 - 45
L-Gln-2-naphthylamide
0.45 - 25
L-Gln-7-amido-4-methylcoumarin
15.7 - 32
L-Gln-Gly-L-Pro
34
L-Gln-L-Arg-Gly-L-Ile-NH2
pH 8.0, 30°C
68
L-Gln-L-Asn-Gly-L-Ile-NH2
pH 8.0, 30°C
13.1 - 40
L-Gln-L-Asp-L-Glu-L-Leu-NH2
14.9 - 64
L-Gln-L-Glu-L-Ala-L-Phe-NH2
49
L-Gln-L-Glu-L-Tyr-L-Ala-NH2
pH 8.0, 30°C
9.2 - 50
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
20.6 - 62
L-Gln-L-Lys-L-Arg-L-Leu-NH2
55 - 57
L-Gln-L-Phe-L-Ala-NH2
44
L-Gln-L-Ser-L-Tyr-L-Phe-NH2
pH 8.0, 30°C
23
L-Gln-L-Thr-Gly-L-Ile-NH2
pH 8.0, 30°C
41
L-Gln-L-Trp-L-Ala-NH2
pH 8.0, 30°C
10.9 - 27
L-Gln-L-Val-L-Ala-NH2
21 - 128
L-Gln-tert-butyl ester
33
L-glutamine tert-butyl ester
-
-
8.8
L-glutaminyl 2-naphthylamide
at pH 8.0 and 25°C
18.8
L-glutaminyl-2-naphthylamide
-
30°C, recombinant enzyme, expressed in Pichia pastoris
5.4
L-glutaminyl-4-methylcoumarinylamide
-
30°C, recombinant enzyme, expressed in Pichia pastoris
1.07 - 7
L-glutaminyl-7-amido-4-methylcoumarin
3.4 - 17.48
L-glutaminyl-beta-naphthylamide
20 - 47.2
N1-naphthalen-2-yl-L-glutamamide
0.25
Nepsilon-(L-gamma-glutamyl)-D-lysine
-
pH and temperature not specified in the publication
0.2
Nepsilon-(L-gamma-glutamyl)-L-lysine
-
pH and temperature not specified in the publication
12
O-(n-butylcarbamyl)-L-serine
-
pH and temperature not specified in the publication
170
QAAR
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.26
S-(cyclohexylamine)-L-cysteine
-
pH and temperature not specified in the publication
0.27
S-(n-butylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
0.24
S-(n-propylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
37.7 - 69.6
[Gln1]-fertilization promoting peptide
-
31.6 - 54.1
[Gln1]-gastrin
-
69.2 - 72.4
[Gln1]-gonadotropin releasing-hormone
-
37.7 - 48.8
[Gln1]-neurotensin
82.8
[Gln1]-thyrotropin releasing-hormone
-
pH 8.0, 30°C
-
41.4
Gln(3)-amyloid-beta peptide 3-11 amide
-
pH 6.0, 30°C, 1% DMSO
-
55
Gln(3)-amyloid-beta peptide 3-11 amide
-
pH 6.0, 30°C, in absence of DMSO
-
0.0019
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D305E
0.0042
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D248Q
0.03
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D305N
0.068
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D305A
0.085
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme D248A
0.84
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme S160G
1
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme E201D
1
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme H319L
5.3
Gln-2-naphthylamide
-
pH 8.0, 25°C, mutant enzyme S160A
5.4
Gln-2-naphthylamide
-
pH 8.0, 25°C, wild-type enzyme
1.27
Gln-Ala
-
-
47.6
Gln-Ala
-
pH 8.0, 30°C, 0.5 M KCl
57.2
Gln-Ala
-
pH 8.0, 30°C
68.1
Gln-Ala
-
pH 8.0, 30°C, 0.5 M KCl
69.8
Gln-Ala
-
pH 8.0, 30°C
60.5
Gln-Ala-Ala-Ala-Ala-NH2
-
pH 8.0, 30°C
74.6
Gln-Ala-Ala-Ala-Ala-NH2
-
pH 8.0, 30°C
76.3
Gln-Ala-Ala-NH2
-
pH 8.0, 30°C
83.2
Gln-Ala-Ala-NH2
-
pH 8.0, 30°C
55.3
Gln-Ala-Ala-Ser-Ala-Ala-NH2
-
pH 8.0, 30°C
78.5
Gln-Ala-Ala-Ser-Ala-Ala-NH2
-
pH 8.0, 30°C
29.8
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C, 0.5 M KCl
33.5
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C
48.4
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C, 0.5 M KCl
49.2
Gln-Arg-Gly-Ile-NH2
-
pH 8.0, 30°C
29.6
Gln-Arg-Tyr-Phe-NH2
-
pH 8.0, 30°C
48.9
Gln-Arg-Tyr-Phe-NH2
-
pH 8.0, 30°C
51.4
Gln-Asn-Gly-Ile-NH2
-
pH 8.0, 30°C
56.6
Gln-Asn-Gly-Ile-NH2
-
pH 8.0, 30°C
0.43
Gln-Gln
pH 8.0, mutant enzyme W207L
0.87
Gln-Gln
pH 8.0, mutant enzyme E201D
1.35
Gln-Gln
pH 8.0, mutant enzyme W329A
2.32
Gln-Gln
pH 8.0, mutant enzyme W207F
2.7
Gln-Gln
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
7.3
Gln-Gln
pH 7.0, wild-type enzyme
7.35
Gln-Gln
pH 8.0, mutant enzyme R54W
7.91
Gln-Gln
pH 8.0, mutant enzyme F146A
8.56
Gln-Gln
pH 8.8, wild-type enzyme
8.63
Gln-Gln
pH 8.0, wild-type enzyme
8.66
Gln-Gln
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
9.39
Gln-Gln
pH 8.0, mutant enzyme Q304L
9.76
Gln-Gln
pH 7.5, wild-type enzyme
9.93
Gln-Gln
pH 8.5, wild-type enzyme
11.67
Gln-Gln
pH 8.0, mutant enzyme K144A
12.91
Gln-Gln
pH 8.0, mutant enzyme F325A
20.7
Gln-Gln
-
pH 8.0, 30°C
43.2
Gln-Gln
-
pH 8.0, 30°C
41.4
Gln-Gln-Tyr-Phe-NH2
-
pH 8.0, 30°C
52.9
Gln-Gln-Tyr-Phe-NH2
-
pH 8.0, 30°C
2.6
Gln-Glu
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
7.79
Gln-Glu
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
18.9
Gln-Glu
-
pH 8.0, 30°C, 0.5 M KCl
24.7
Gln-Glu
-
pH 8.0, 30°C
44.4
Gln-Glu
-
pH 8.0, 30°C, 0.5 M KCl
50.3
Gln-Glu
-
pH 8.0, 30°C
46
Gln-Glu-Ala-Ala-NH2
-
pH 8.0, 30°C
53.7
Gln-Glu-Ala-Ala-NH2
-
pH 8.0, 30°C
39
Gln-Glu-Ala-Phe-NH2
-
pH 8.0, 30°C
48.5
Gln-Glu-Ala-Phe-NH2
-
pH 8.0, 30°C
45.6
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
45.8
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C
53.6
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
58.5
Gln-Glu-Asp-Leu-NH2
-
pH 8.0, 30°C
42.1
Gln-Glu-Tyr-Ala-NH2
-
pH 8.0, 30°C
44.7
Gln-Glu-Tyr-Ala-NH2
-
pH 8.0, 30°C
45.1
Gln-Glu-Tyr-NH2
-
pH 8.0, 30°C
53.6
Gln-Glu-Tyr-NH2
-
pH 8.0, 30°C
46
Gln-Glu-Tyr-Phe-NH2
-
pH 8.0, 30°C
54.6
Gln-Glu-Tyr-Phe-NH2
-
pH 8.0, 30°C
0.368
Gln-Gly
-
-
1.65
Gln-Gly
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
4.57
Gln-Gly
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
13.2
Gln-Gly
-
pH 8.0, 30°C
45.8
Gln-Gly
-
pH 8.0, 30°C
4
Gln-Gly-Pro
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
11.4
Gln-Gly-Pro
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
25.3
Gln-Gly-Pro
-
pH 8.0, 30°C
41.7
Gln-Gly-Pro
-
pH 8.0, 30°C
55.4
Gln-His-Tyr-Phe-NH2
-
pH 8.0, 30°C
75.9
Gln-His-Tyr-Phe-NH2
-
pH 8.0, 30°C
31.6
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
33.4
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C
48.2
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C
58.1
Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C, 0.5 M KCl
0.36
Gln-NH2
-
mutant enzyme H319Q
0.388
Gln-NH2
-
mutant enzyme H307Q
0.435
Gln-NH2
-
unmutated enzyme
12.2
Gln-NH2
-
pH 8.0, 30°C, 0.5 M KCl
12.8
Gln-NH2
-
pH 8.0, 30°C
20.7
Gln-NH2
-
30°C, recombinant enzyme, expressed in Pichia pastoris
44.8
Gln-NH2
-
pH 8.0, 30°C
45.2
Gln-NH2
-
pH 8.0, 30°C, 0.5 M KCl
7.5
Gln-Phe-Ala
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
24.1
Gln-Phe-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
109
Gln-Phe-Ala-NH2
-
pH 8.0, 30°C
132
Gln-Phe-Ala-NH2
-
pH 8.0, 30°C
18.8
Gln-Pro-Tyr-Phe-NH2
-
pH 8.0, 30°C
31.7
Gln-Pro-Tyr-Phe-NH2
-
pH 8.0, 30°C
52.8
Gln-Ser-Tyr-Phe-NH2
-
pH 8.0, 30°C
64.9
Gln-Ser-Tyr-Phe-NH2
-
pH 8.0, 30°C
6.7
Gln-tert-butyl ester
-
pH 8.0, 30°C
16
Gln-tert-butyl ester
-
-
20.9
Gln-tert-butyl ester
-
-
49.4
Gln-tert-butyl ester
-
pH 8.0, 30°C
47
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C
50
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C, 0.5 M KCl
133
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C, 0.5 M KCl
151.8
Gln-Trp-Ala-NH2
-
pH 8.0, 30°C
7.7
Gln-Tyr-Ala
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
22.9
Gln-Tyr-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
104
Gln-Tyr-Ala
-
pH 8.0, 30°C
125
Gln-Tyr-Ala
-
pH 8.0, 30°C
125
Gln-Tyr-Ala-OH
-
30°C, recombinant enzyme, expressed in Pichia pastoris
220
Gln-Tyr-Ala-OH
-
37°C, recombinant enzyme, expressed in Pichia pastoris
1.07
H-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
19
H-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
25
H-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
16
H-Gln-Ala-OH
30°C, isoDromeQC
30
H-Gln-Ala-OH
-
pH 8.0, 30°C
37.7
H-Gln-Ala-OH
pH 8.0, 30°C
13.1
H-Gln-Asp-Glu-Leu-NH2
-
pH 8.0, 30°C
14
H-Gln-Asp-Glu-Leu-NH2
30°C
40
H-Gln-Asp-Glu-Leu-NH2
pH 8.0, 30°C
1.1
H-Gln-beta-naphthylamide
30°C, isoDromeQC
1.3
H-Gln-beta-naphthylamide
30°C
3.4
H-Gln-beta-naphthylamide
-
pH 8.0, 30°C
8
H-Gln-beta-naphthylamide
-
pH 8.0, 30°C
45
H-Gln-beta-naphthylamide
pH 8.0, 30°C
2.72
H-Gln-Gln-OH
-
pH 8.0, 30°C
7.4
H-Gln-Gln-OH
30°C, isoDromeQC
17
H-Gln-Gln-OH
-
pH 8.0, 30°C
24
H-Gln-Gln-OH
pH 8.0, 30°C
11
H-Gln-Glu-Ala-Phe-NH2
30°C, isoDromeQC
12.7
H-Gln-Glu-Ala-Phe-NH2
30°C
14.9
H-Gln-Glu-Ala-Phe-NH2
-
pH 8.0, 30°C
64
H-Gln-Glu-Ala-Phe-NH2
pH 8.0, 30°C
2.65
H-Gln-Glu-OH
-
pH 8.0, 30°C
16.4
H-Gln-Glu-OH
-
pH 8.0, 30°C
30
H-Gln-Glu-OH
pH 8.0, 30°C
6.9
H-Gln-Glu-Tyr-Phe-NH2
30°C
9.2
H-Gln-Glu-Tyr-Phe-NH2
-
pH 8.0, 30°C
50
H-Gln-Glu-Tyr-Phe-NH2
pH 8.0, 30°C
1.66
H-Gln-Gly-OH
-
pH 8.0, 30°C
2 - 8
H-Gln-Gly-OH
pH 8.0, 30°C
4.9
H-Gln-Gly-OH
30°C, isoDromeQC
22
H-Gln-Gly-OH
-
pH 8.0, 30°C
4.02
H-Gln-Gly-Pro-OH
-
pH 8.0, 30°C
14
H-Gln-Gly-Pro-OH
30°C, isoDromeQC
15.7
H-Gln-Gly-Pro-OH
-
pH 8.0, 30°C
32
H-Gln-Gly-Pro-OH
pH 8.0, 30°C
7
H-Gln-Lys-Arg-Leu-NH2
30°C
20.6
H-Gln-Lys-Arg-Leu-NH2
-
pH 8.0, 30°C
62
H-Gln-Lys-Arg-Leu-NH2
pH 8.0, 30°C
25
H-Gln-NH2
-
pH 8.0, 30°C
37
H-Gln-NH2
pH 8.0, 30°C
55
H-Gln-Phe-Ala-NH2
-
pH 8.0, 30°C
57
H-Gln-Phe-Ala-NH2
pH 8.0, 30°C
16
H-Gln-Phe-Ala-OH
30°C, isoDromeQC
3.02
H-Gln-Val-Ala-OH
30°C, isoDromeQC
5.3
H-Gln-Val-Ala-OH
30°C
10.9
H-Gln-Val-Ala-OH
-
pH 8.0, 30°C
27
H-Gln-Val-Ala-OH
pH 8.0, 30°C
1.4
L-Gln-2-naphthylamide
wild type enzyme, at pH 7.0 at 25°C
2.7
L-Gln-2-naphthylamide
in 0.1 M MES, pH 6.0, temperature not specified in the publication
5.8
L-Gln-2-naphthylamide
mutant enzyme E45Q, at pH 7.0 at 25°C
8
L-Gln-2-naphthylamide
-
pH 8.0, 30°C
18.9
L-Gln-2-naphthylamide
in 0.1 M MES, pH 7.5, temperature not specified in the publication
22
L-Gln-2-naphthylamide
pH 8.0, 30°C
45
L-Gln-2-naphthylamide
pH 8.0, 30°C
0.45
L-Gln-7-amido-4-methylcoumarin
in 0.1 M MES, pH 6.0, temperature not specified in the publication
6
L-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
7.1
L-Gln-7-amido-4-methylcoumarin
in 0.1 M MES, pH 7.5, temperature not specified in the publication
19
L-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
25
L-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
35.7
L-Gln-amide
in 0.1 M MES, pH 7.5, temperature not specified in the publication
61.5
L-Gln-amide
in 0.1 M MES, pH 6.0, temperature not specified in the publication
2 - 8
L-Gln-Gly
pH 8.0, 30°C
12.4
L-Gln-Gly
pH 8.0, 30°C
22
L-Gln-Gly
-
pH 8.0, 30°C
32
L-Gln-Gly
in 0.1 M MES, pH 6.0, temperature not specified in the publication
15.7
L-Gln-Gly-L-Pro
-
pH 8.0, 30°C
21.6
L-Gln-Gly-L-Pro
pH 8.0, 30°C
32
L-Gln-Gly-L-Pro
pH 8.0, 30°C
30
L-Gln-L-Ala
-
pH 8.0, 30°C
37.7
L-Gln-L-Ala
pH 8.0, 30°C
42
L-Gln-L-Ala
pH 8.0, 30°C
13.1
L-Gln-L-Asp-L-Glu-L-Leu-NH2
-
pH 8.0, 30°C
40
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pH 8.0, 30°C
0.27
L-Gln-L-Gln
in 0.1 M MES, pH 6.0, temperature not specified in the publication
17
L-Gln-L-Gln
-
pH 8.0, 30°C
24
L-Gln-L-Gln
pH 8.0, 30°C
31.7
L-Gln-L-Gln
in 0.1 M MES, pH 7.5, temperature not specified in the publication
32
L-Gln-L-Gln
pH 8.0, 30°C
0.021
L-Gln-L-Glu
in 0.1 M MES, pH 6.0, temperature not specified in the publication
12.8
L-Gln-L-Glu
in 0.1 M MES, pH 7.5, temperature not specified in the publication
16.4
L-Gln-L-Glu
-
pH 8.0, 30°C
29
L-Gln-L-Glu
pH 8.0, 30°C
30
L-Gln-L-Glu
pH 8.0, 30°C
14.9
L-Gln-L-Glu-L-Ala-L-Phe-NH2
-
pH 8.0, 30°C
64
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pH 8.0, 30°C
9.2
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
-
pH 8.0, 30°C
50
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pH 8.0, 30°C
20.6
L-Gln-L-Lys-L-Arg-L-Leu-NH2
-
pH 8.0, 30°C
62
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pH 8.0, 30°C
55
L-Gln-L-Phe-L-Ala-NH2
-
pH 8.0, 30°C
57
L-Gln-L-Phe-L-Ala-NH2
pH 8.0, 30°C
10.9
L-Gln-L-Val-L-Ala-NH2
-
pH 8.0, 30°C
27
L-Gln-L-Val-L-Ala-NH2
pH 8.0, 30°C
25
L-Gln-NH2
-
pH 8.0, 30°C
37
L-Gln-NH2
pH 8.0, 30°C
21
L-Gln-tert-butyl ester
-
pH 8.0, 30°C
31.3
L-Gln-tert-butyl ester
pH 8.0, 30°C
64.9
L-Gln-tert-butyl ester
in 0.1 M MES, pH 7.5, temperature not specified in the publication
128
L-Gln-tert-butyl ester
in 0.1 M MES, pH 6.0, temperature not specified in the publication
1.07
L-glutaminyl-7-amido-4-methylcoumarin
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
2.09
L-glutaminyl-7-amido-4-methylcoumarin
30°C, isoDromeQC
6.98
L-glutaminyl-7-amido-4-methylcoumarin
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
7
L-glutaminyl-7-amido-4-methylcoumarin
30°C
3.4
L-glutaminyl-beta-naphthylamide
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
17.48
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
20
N1-naphthalen-2-yl-L-glutamamide
-
pH 8.0, 30°C, 0.5 M KCl
47.2
N1-naphthalen-2-yl-L-glutamamide
-
pH 8.0, 30°C, 0.5 M KCl
0.054
QAAE
in 0.1 M MES, pH 6.0, temperature not specified in the publication
40
QAAE
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.00008
QAAF
in 0.1 M MES, pH 6.0, temperature not specified in the publication
183
QAAF
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0042
QAEA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
40
QAEA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0064
QAFA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
102
QAFA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0032
QARA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
129
QARA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.007
QEAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
17.9
QEAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
6.4
QEDL
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
6.4
QEDL
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
3.3
QEYF
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
11.78
QEYF
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.084
QFAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
60
QFAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
30
QFRH-NH2
-
at pH 6.5
0.012
QGGG
in 0.1 M MES, pH 6.0, temperature not specified in the publication
1.1
QGGG
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0074
QRAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
66
QRAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
37.7
[Gln1]-fertilization promoting peptide
-
pH 8.0, 30°C
-
69.6
[Gln1]-fertilization promoting peptide
-
pH 8.0, 30°C
-
31.6
[Gln1]-gastrin
-
pH 8.0, 30°C
-
54.1
[Gln1]-gastrin
-
pH 8.0, 30°C
-
69.2
[Gln1]-gonadotropin releasing-hormone
-
pH 8.0, 30°C
-
72.4
[Gln1]-gonadotropin releasing-hormone
-
pH 8.0, 30°C
-
37.7
[Gln1]-neurotensin
-
pH 8.0, 30°C
48.8
[Gln1]-neurotensin
-
pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.058
2-amino-5-(butan-2-ylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.19
2-amino-5-(cyclohexylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.21
2-amino-5-(cyclopropylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.097
2-amino-5-oxo-5-(propan-2-ylamino)pentanoic acid
-
pH and temperature not specified in the publication
0.38
2-amino-5-oxo-5-[(2-phenylethyl)amino]pentanoic acid
-
pH and temperature not specified in the publication
0.51
2-amino-5-[(2-methylbutyl)amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.066
2-amino-5-[(2S)-butan-2-ylamino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.55
2-amino-5-[[(2S)-2-methylbutyl]amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
15.9 - 49.9
39SrpL21 protein
-
7.8 - 73.1
ALDH2 protein
-
13.9 - 59.3
DIM-10 protein
-
0.000019 - 0.00074
EFRH-NH2
0.000073 - 0.00009
EFRHHDSGYE-NH2
0.39
L-gamma-glutamyl-(+)-3-aminobutyric acid
-
pH and temperature not specified in the publication
0.21
L-gamma-glutamyl-(+)-3-aminoisobutyric acid
-
pH and temperature not specified in the publication
0.19
L-gamma-glutamyl-beta-alanine
-
pH and temperature not specified in the publication
0.11
L-gamma-glutamyl-ethylamine
-
pH and temperature not specified in the publication
0.83
L-gamma-glutamyl-n-butylamine
-
pH and temperature not specified in the publication
0.72
L-gamma-glutamyl-n-propylamine
-
pH and temperature not specified in the publication
0.35
L-gamma-glutamylaniline
-
pH and temperature not specified in the publication
0.71
L-gamma-glutamylbenzylamine
-
pH and temperature not specified in the publication
0.9
L-gamma-glutamylcyclopentylamine
-
pH and temperature not specified in the publication
0.071
L-gamma-glutamylglycine
-
pH and temperature not specified in the publication
1.45
L-gamma-glutamylneohexylamine
-
pH and temperature not specified in the publication
0.057
L-gamma-glutamylneopentylamine
-
pH and temperature not specified in the publication
6.64 - 166.1
L-Gln-2-naphthylamide
1.46 - 142
L-Gln-7-amido-4-methylcoumarin
8.5
L-Gln-Gly
in 0.1 M MES, pH 6.0, temperature not specified in the publication
15.7 - 63.6
L-Gln-tert-butyl ester
103 - 311
L-glutaminyl-7-amido-4-methylcoumarin
229 - 554
L-glutaminyl-beta-naphthylamide
0.92
Nepsilon-(L-gamma-glutamyl)-D-lysine
-
pH and temperature not specified in the publication
0.78
Nepsilon-(L-gamma-glutamyl)-L-lysine
-
pH and temperature not specified in the publication
4.2 - 23.8
NPLP4 protein
-
0.6
O-(n-butylcarbamyl)-L-serine
-
pH and temperature not specified in the publication
412
QAAR
in 0.1 M MES, pH 7.5, temperature not specified in the publication
26.2 - 88
rho-7 protein
-
1.5
S-(cyclohexylamine)-L-cysteine
-
pH and temperature not specified in the publication
2.8
S-(n-butylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
2.6
S-(n-propylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
15.9
39SrpL21 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
20.2
39SrpL21 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
20.9
39SrpL21 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)
-
21.1
39SrpL21 protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
21.9
39SrpL21 protein
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
27.6
39SrpL21 protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
45.3
39SrpL21 protein
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
49.9
39SrpL21 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)
-
35
Acp33A protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
36
Acp33A protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
36.9
Acp33A protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
38
Acp33A protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
7.8
ALDH2 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
8.3
ALDH2 protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
26.2
ALDH2 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
32
ALDH2 protein
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
33.9
ALDH2 protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
40.9
ALDH2 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)
-
69
ALDH2 protein
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
73.1
ALDH2 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)
-
13.9
DIM-10 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
17.5
DIM-10 protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
25.9
DIM-10 protein
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
31.2
DIM-10 protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
31.2
DIM-10 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)
-
43.3
DIM-10 protein
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
50.7
DIM-10 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)
-
59.3
DIM-10 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
0.000019
EFRH-NH2
-
at pH 6.5
0.000037
EFRH-NH2
-
at pH 6.5
0.00017
EFRH-NH2
-
at pH 6.5
0.00074
EFRH-NH2
-
at pH 6.5
0.000073
EFRHHDSGYE-NH2
-
at low substrate concentrations
0.00009
EFRHHDSGYE-NH2
-
-
54
Gln-Gln
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
95
Gln-Gln
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
9
Gln-Glu
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
16
Gln-Glu
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
9
Gln-Gly
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
28
Gln-Gly
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
38
Gln-Gly-Pro
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
111
Gln-Gly-Pro
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
117
Gln-Phe-Ala
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
403
Gln-Phe-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
207
Gln-Tyr-Ala
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
394
Gln-Tyr-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
6.64
L-Gln-2-naphthylamide
in 0.1 M MES, pH 6.0, temperature not specified in the publication
12.6
L-Gln-2-naphthylamide
wild type enzyme, at pH 7.0 at 25°C
35
L-Gln-2-naphthylamide
in 0.1 M MES, pH 7.5, temperature not specified in the publication
166.1
L-Gln-2-naphthylamide
mutant enzyme E45Q, at pH 7.0 at 25°C
1.46
L-Gln-7-amido-4-methylcoumarin
in 0.1 M MES, pH 6.0, temperature not specified in the publication
142
L-Gln-7-amido-4-methylcoumarin
in 0.1 M MES, pH 7.5, temperature not specified in the publication
13
L-Gln-amide
in 0.1 M MES, pH 7.5, temperature not specified in the publication
21.2
L-Gln-amide
in 0.1 M MES, pH 6.0, temperature not specified in the publication
0.013
L-Gln-L-Gln
in 0.1 M MES, pH 6.0, temperature not specified in the publication
4.8
L-Gln-L-Gln
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0049
L-Gln-L-Glu
in 0.1 M MES, pH 6.0, temperature not specified in the publication
5.4
L-Gln-L-Glu
in 0.1 M MES, pH 7.5, temperature not specified in the publication
15.7
L-Gln-tert-butyl ester
in 0.1 M MES, pH 6.0, temperature not specified in the publication
63.6
L-Gln-tert-butyl ester
in 0.1 M MES, pH 7.5, temperature not specified in the publication
103
L-glutaminyl-7-amido-4-methylcoumarin
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
311
L-glutaminyl-7-amido-4-methylcoumarin
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
229
L-glutaminyl-beta-naphthylamide
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
554
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
22
MCCB protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
22.8
MCCB protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
25
MCCB protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)
-
25.5
MCCB protein
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
26.1
MCCB protein
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
28.9
MCCB protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)
-
32.3
MCCB protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
33.2
MCCB protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
4.2
NPLP4 protein
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
4.6
NPLP4 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)
-
6
NPLP4 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)
-
7.4
NPLP4 protein
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
20.1
NPLP4 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
20.9
NPLP4 protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
21.5
NPLP4 protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
23.8
NPLP4 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
0.034
QAAE
in 0.1 M MES, pH 6.0, temperature not specified in the publication
36
QAAE
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0008
QAAF
in 0.1 M MES, pH 6.0, temperature not specified in the publication
219
QAAF
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.02
QAEA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
55
QAEA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0031
QAFA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
41
QAFA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0013
QARA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
1215
QARA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0067
QEAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
18
QEAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
55
QEDL
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
104
QEDL
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
123
QEYF
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
413
QEYF
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.24
QFAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
31
QFAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
98.9
QFRH-NH2
-
at pH 6.5
0.0021
QGGG
in 0.1 M MES, pH 6.0, temperature not specified in the publication
9
QGGG
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.0026
QRAA
in 0.1 M MES, pH 6.0, temperature not specified in the publication
76
QRAA
in 0.1 M MES, pH 7.5, temperature not specified in the publication
26.2
rho-7 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)
-
30.2
rho-7 protein
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
40.9
rho-7 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)
-
43.4
rho-7 protein
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
-
50.2
rho-7 protein
isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)
-
53.3
rho-7 protein
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
55
rho-7 protein
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
-
88
rho-7 protein
isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.253
(3,4-dichlorophenyl)-2-cyano-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)guanidine
-
0.62
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
1.36
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(3,4-dimethoxyphenyl)guanidine
-
6.72
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(4-(trifluoromethyl)phenyl)guanidine
-
0.83
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(4-isopropylphenyl)guanidine
-
0.7
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(4-methoxyphenyl)guanidine
-
1.37
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(cyclopropylmethyl)guanidine
-
1.53
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-methylguanidine
-
1.02
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-phenylguanidine
-
1.09
(3-(1H-imidazol-1-yl)propyl)-3-(4-bromophenyl)-2-cyanoguanidine
-
1.65
(3-(4-methyl-1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
0.13
(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
0.00345
1,10-phenanthroline
at pH 8.0 and 25°C
0.295
1,4-bis-(imidazol-1-yl)methyl-2,5-dimethylbenzene
30°C, pH 8.0
0.00112
1-(2,3-dihydro-1,4-benzodioxin-6-yl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.00056
1-(2,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.184
1-(2-oxo-2-phenylethyl)-imidazole
30°C, pH 8.0
0.00155
1-(3,4-dimethoxybenzyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.00233
1-(3,4-dimethoxyphenyl)-3-(2-[1-(1H-imidazol-1-yl)cyclopropyl]ethyl)thiourea
-
pH 8.0, 30°C
0.06
1-(3,4-dimethoxyphenyl)-3-(3-(4-methyl-1H-imidazol-1-yl)propyl)thiourea
-
0.0063
1-(3,4-dimethoxyphenyl)-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
-
0.00034
1-(3,4-dimethoxyphenyl)-3-[(3R)-3-(1H-imidazol-1-yl)butyl]thiourea
-
pH 8.0, 30°C
0.00076
1-(3,4-dimethoxyphenyl)-3-[(3S)-3-(1H-imidazol-1-yl)butyl]thiourea
-
pH 8.0, 30°C
0.00006
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.00049
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]urea
-
pH 8.0, 30°C
0.00055
1-(3,4-dimethoxyphenyl)-3-[4-(1H-imidazol-1-yl)butyl]thiourea
-
pH 8.0, 30°C
0.041
1-(3,4-dimethoxyphenyl)-N-(3-(4-methyl-1H-imidazol-1-yl)propyl)cyclopropanecarbothioamide
-
0.0026
1-(3,4-dimethoxyphenyl)-N-(3-(5-methyl-1H-imidazol-1-yl)propyl)cyclopropanecarbothioamide
-
0.00075
1-(3,5-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.41
1-(3-aminopropyl)-imidazole
30°C, pH 8.0
0.0018
1-(4-acetylphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.00089
1-(4-ethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.0028
1-(4-ethylphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.0062
1-(6-phenoxyhexyl)-1H-imidazole
-
0.000262 - 0.114
1-Benzylimidazole
0.12
1-methyl-5-(beta-aminoethyl)-imidazole
30°C, pH 8.0
0.000101 - 0.109
1-Methylimidazole
0.049
1-vinylimidazole
30°C, pH 8.0
0.0028
1-[3-(1H-imidazol-1-yl)propyl]-3-(1-naphthyl)thiourea
-
pH 8.0, 30°C
0.00034
1-[3-(1H-imidazol-1-yl)propyl]-3-(3,4,5-trimethoxyphenyl)thiourea
-
pH 8.0, 30°C
0.00186
1-[3-(1H-imidazol-1-yl)propyl]-3-(3-methoxyphenyl)thiourea
-
pH 8.0, 30°C
0.0007
1-[3-(1H-imidazol-1-yl)propyl]-3-(4-methoxyphenyl)thiourea
-
pH 8.0, 30°C
0.00214
1-[3-(1H-imidazol-1-yl)propyl]-3-(4-methylphenyl)thiourea
-
pH 8.0, 30°C
0.00166
1-[3-(1H-imidazol-1-yl)propyl]-3-[4-(methylthio)phenyl]thiourea
-
pH 8.0, 30°C
0.00097
1-[4-(benzyloxy)phenyl]-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
pH 8.0, 30°C
0.23
2,3-dihydro-3-(3-(4-methyl-1H-imidazol-1-yl)propyl)-2-thioxoquinazolin-4(1H)-one
-
0.018
2,3-dihydro-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-thioxoquinazolin-4(1H)-one
-
0.083
2,3-dihydro-6-methyl-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-5-phenyl-2-thioxothieno[2,3-d]pyrimidin-4(1H)-one
-
1.8
2-aminobenzimidazole
30°C, pH 8.0
0.061
2-cyano(3,4,5-trimethoxyphenyl)-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)guanidine
-
0.082
2-cyano(3-(5-methyl-1H-imidazol-1-yl)propyl)-3-(3,4-dimethylphenyl)guanidine
-
0.065
2-cyano-1-[3-(5-methyl-1H-imidazol-1-yl)propyl]-4-phenylbenzene-1-guanidine
-
0.58
2-ethyl-4-methyl-imidazole
30°C, pH 8.0
0.165
2-methyl-benzylimidazole
30°C, pH 8.0
0.3
3-(3-(1H-imidazol-1-yl)propyl)-2,3-dihydro-2-thioxoquinazolin-4(1H)-one
-
0.36
3-(3-(1H-imidazol-1-yl)propyl)-2,3-dihydro-7-methyl-2-thioxothieno[3,2-d]pyrimidin-4(1H)-one
-
0.62
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-1,2,3,5,6,7-hexahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
-
0.9
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8,9,10-octahydrocycloocta[4,5]thieno[2,3-d]pyrimidin-4(1H)-one
-
0.34
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
0.818
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxoimidazolidin-4-one
30°C, pH 8.0
0.039
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8,9,10-octahydrocycloocta[4,5]-thieno[2,3-d]pyrimidin-4(1H)-one
-
0.017
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
0.0023
4-(2-imidazol-1-yl-ethoxy)-benzoic acid
30°C, pH 8.0
7.6
4-imidazole-carboxaldehyde
30°C, pH 8.0
0.073
4-methylimidazole
pH 8
0.000023
5-(5-[[(3,4-dimethoxyphenyl)sulfanyl]methyl]-1,3,4-oxadiazol-2-yl)-1H-benzimidazole
pH and temperature not specified in the publication
0.00101
5-(5-[[(pyridin-4-yl)methyl]sulfanyl]-1,3,4-oxadiazol-2-yl)-1H-benzimidazole
pH and temperature not specified in the publication
15.5
5-amino-3H-imidazole-4-carboxylic acid amide
30°C, pH 8.0
0.129
5-hydroxymethyl-4-methyl-imidazole
30°C, pH 8.0
0.000638
5-[5-(2-phenylethyl)-1,3,4-oxadiazol-2-yl]-1H-benzimidazole
pH and temperature not specified in the publication
0.02
6-benzyl-2,3-dihydro-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-thioxothieno[2,3-d]pyrimidin-4(1H)-one
-
0.017 - 2.188
benzimidazole
0.0035 - 0.0073
benzylimidazole
0.0368
dipicolinic acid
at pH 8.0 and 25°C
4.69 - 10.4
EFRHHDSGYE-NH2
0.97 - 1.33
Gln-tert-butyl ester
4.5 - 5.73
H-Gln-7-amido-4-methylcoumarin
1.3 - 1.47
H-Gln-beta-naphthylamide
0.6
H-His-Trp-OH
30°C, pH 8.0
14.5
imidazol-4-carbonic acid methylester
30°C, pH 8.0
1.54 - 5.06
L-Gln-2-naphthylamide
4.47
L-glutaminyl-7-amido-4-methylcoumarin
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
1.57 - 3.55
L-glutaminyl-beta-naphthylamide
0.85
L-histamine
30°C, pH 8.0
0.56
L-histidinamide
30°C, pH 8.0
4.4
L-histidine
30°C, pH 8.0
1.53
L-histidinol
30°C, pH 8.0
0.023 - 0.082
methylimidazole
0.027
N,N-dimethylcysteamine
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.051
N-(-1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-chloro-benzenamine
-
0.54
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
0.61
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-3,4-dimethoxy-benzenamine
-
0.54
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-(trifluoromethyl)-benzenamine
-
0.57
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-chlorobenzenamine
-
1.03
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-methoxybenzenamine
-
1.17
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)benzenamine
-
0.52
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)naphthalen-1-amine
-
1.29
N-(1-(3-(4-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
0.067
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
0.034
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-(trifluoromethyl)benzenamine
-
0.044
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)cyclohexanamine
-
0.042
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)naphthalen-1-amine
-
0.000006
N-(3,4-dimethoxyphenyl)-N'-[3-(1H-imidazol-1-yl)propyl]thiourea
pH and temperature not specified in the publication
0.5
N-(3-(1H-imidazol-1-yl)propyl)-N-cyclohexyl-2-nitroethene-1,1-diamine
-
20.55
N-(3-(1H-imidazol-1-yl)propyl)-N-methyl-2-nitroethene-1,1-diamine
-
0.0012
N-(4-chlorophenyl)-N'-[2-(1H-imidazol-1-yl)propyl]-2-thioxoimidazolidin-4-one
30°C, pH 8.0
0.00124
N-(4-chlorophenyl)-N'-[3-(1H-imidazol-1-yl)propyl]thiourea
pH and temperature not specified in the publication
0.167
N-(trimethylsilyl)-imidazole
30°C, pH 8.0
0.107
N-Acetylimidazole
30°C, pH 8.0
0.174
N-benzoylimidazole
30°C, pH 8.0
0.0109 - 0.405
N-diethylcysteamine
0.022 - 0.08
N-dimethylcysteamine
0.013
N-methylimidazole
-
pH 8.0, 30°C
0.017 - 0.827
N-omega-acetylhistamine
0.002
N-[3-(1H-imidazol-1-yl)propyl]-5-methoxy-1,3-benzothiazol-2-amine
-
pH 8.0, 30°C
0.00157
N-[3-(1H-imidazol-1-yl)propyl]-6-methoxy-1,3-benzothiazol-2-amine
-
pH 8.0, 30°C
0.001698 - 0.0142
Nomega-acetylhistamine
0.078
oxalic acid diimidazolidide
30°C, pH 8.0
0.000097 - 0.145
P150/03
-
0.000095 - 0.003139
PBD150
0.00002
SEN177
pH 8.0, 25°C, with enzyme mutant Y115E/Y117E
additional information
additional information
-
0.000262
1-Benzylimidazole
Golgi-resident glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.000607
1-Benzylimidazole
secretory glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.0071
1-Benzylimidazole
30°C, pH 8.0
0.0102
1-Benzylimidazole
at pH 8.0 and 25°C
0.013
1-Benzylimidazole
pH 7
0.019
1-Benzylimidazole
pH 8, isoDromeQC
0.048
1-Benzylimidazole
pH 8
0.114
1-Benzylimidazole
pH 7, isoDromeQC
0.000101
1-Methylimidazole
pH 7, isoDromeQC
0.03
1-Methylimidazole
30°C, pH 8.0
0.036
1-Methylimidazole
pH 7
0.103
1-Methylimidazole
pH 8, isoDromeQC
0.109
1-Methylimidazole
pH 8
0.017
benzimidazole
pH 7, isoDromeQC
0.124
benzimidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.13
benzimidazole
-
pH 8.0, 30°C
0.138
benzimidazole
30°C, pH 8.0
0.192
benzimidazole
pH 8.0, 30°C
0.199
benzimidazole
-
pH 8.0, 30°C
0.25
benzimidazole
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
1.145
benzimidazole
pH 8, isoDromeQC
0.0035
benzylimidazole
-
pH 8.0, 30°C
0.0039
benzylimidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.0062
benzylimidazole
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.0064
benzylimidazole
pH 8.0, 30°C
0.0073
benzylimidazole
-
pH 8.0, 30°C
1.824
cacodylate
secretory glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
6.696
cacodylate
Golgi-resident glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.042
cysteamine
pH 8.0, 30°C
0.068
cysteamine
-
pH 8.0, 30°C
0.069
cysteamine
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.154
cysteamine
pH 7, isoDromeQC
0.205
cysteamine
pH 8, isoDromeQC
3.25
EFRH-NH2
-
at pH 8.0
8.33
EFRH-NH2
-
at pH 8.0
24.64
EFRH-NH2
-
at pH 6.0
35.75
EFRH-NH2
-
at pH 6.0
4.69
EFRHHDSGYE-NH2
-
at pH 8.0
6.1
EFRHHDSGYE-NH2
-
at pH 8.0
8.32
EFRHHDSGYE-NH2
-
at pH 6.0
10.4
EFRHHDSGYE-NH2
-
at pH 6.0
0.97
Gln-tert-butyl ester
-
pH 8.0, 30°C, 0.5 M KCl
1.2
Gln-tert-butyl ester
-
pH 8.0, 30°C
1.21
Gln-tert-butyl ester
-
pH 8.0, 30°C
1.33
Gln-tert-butyl ester
-
pH 8.0, 30°C, 0.5 M KCl
4.5
H-Gln-7-amido-4-methylcoumarin
-
pH 8.0, 30°C
5.73
H-Gln-7-amido-4-methylcoumarin
-
-
1.3
H-Gln-beta-naphthylamide
-
pH 8.0, 30°C
1.47
H-Gln-beta-naphthylamide
-
-
0.103
imidazole
30°C, pH 8.0
0.103
imidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.116
imidazole
-
pH 8.0, 30°C
0.16
imidazole
pH 8.0, 30°C
0.219
imidazole
-
pH 8.0, 30°C
0.235
imidazole
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.364
imidazole
pH 8, isoDromeQC
0.671
imidazole
pH 7, isoDromeQC
1.54
L-Gln-2-naphthylamide
wild type enzyme, at pH 7.0 at 25°C
5.06
L-Gln-2-naphthylamide
mutant enzyme E45Q, at pH 7.0 at 25°C
1.57
L-glutaminyl-beta-naphthylamide
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
3.55
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.023
methylimidazole
pH 8.0, 30°C
0.052
methylimidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.079
methylimidazole
-
pH 8.0, 30°C
0.082
methylimidazole
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.0109
N-diethylcysteamine
-
0.093
N-diethylcysteamine
pH 8
0.405
N-diethylcysteamine
pH 8, isoDromeQC
0.022
N-dimethylcysteamine
-
pH 8.0, 30°C
0.029
N-dimethylcysteamine
-
0.063
N-dimethylcysteamine
pH 8, isoDromeQC
0.079
N-dimethylcysteamine
pH 8
0.08
N-dimethylcysteamine
pH 7
0.017
N-omega-acetylhistamine
30°C, pH 8.0
0.0391
N-omega-acetylhistamine
pH 7
0.084
N-omega-acetylhistamine
pH 8
0.14
N-omega-acetylhistamine
pH 8, isoDromeQC
0.827
N-omega-acetylhistamine
pH 7, isoDromeQC
0.001698
Nomega-acetylhistamine
secretory glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.005748
Nomega-acetylhistamine
Golgi-resident glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.0142
Nomega-acetylhistamine
at pH 8.0 and 25°C
0.000097
P150/03
pH 8, isoDromeQC
-
0.145
P150/03
pH 7, isoDromeQC
-
0.000095
PBD150
secretory glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.0001
PBD150
-
pH 8.0, 30°C
0.0001
PBD150
wild type enzyme, in 50 mM Tris, pH 8.0, at 30°C
0.0001013
PBD150
isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)
0.0001093
PBD150
isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)
0.000114
PBD150
wild type enzyme, in 50 mM Tris, pH 8.0, at 30°C
0.000342
PBD150
at pH 8.0 and 25°C
0.0003706
PBD150
isoform isoDromeQC, at 30°C in 50 mM MES (pH 6.0)
0.000944
PBD150
isoform DromeQC, at 30°C in 50 mM MOPS (pH 7.0)
0.001817
PBD150
Golgi-resident glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0
0.00248
PBD150
isoform DromeQC, at 30°C in 50 mM MES (pH 6.0)
0.003139
PBD150
isoform DromeQC, at 30°C in 50 mM Tris (pH 8.0)
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003
5,6-dimethoxy-N-[3-(5-methyl-1H-imidazol-1-yl)propyl]-1,3-benzothiazol-2-amine
Homo sapiens
pH 7.0, 37°C
0.00011
5,6-dimethoxy-N-[3-(5-methyl-1H-imidazol-1-yl)propyl]-1H-benzimidazol-2-amine
Homo sapiens
pH 7.0, 37°C
0.00007
5-(5-[[(3,4-dimethoxyphenyl)sulfanyl]methyl]-1,3,4-oxadiazol-2-yl)-1H-benzimidazole
Homo sapiens
pH and temperature not specified in the publication
0.00396
5-[5-(2-phenylethyl)-1,3,4-oxadiazol-2-yl]-1H-benzimidazole
Homo sapiens
pH and temperature not specified in the publication
0.00064
methyl N-[(2S)-1-hydroxy-2-[[3-(5-methyl-1H-imidazol-1-yl)propyl]amino]-3-phenylpropyl]-L-alaninate
Homo sapiens
pH 7.0, 37°C
0.0000064
N-((E)-4-(3-(4-(2-aminoethyl)piperazin-1-yl)-3-oxoprop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000194
N-((E)-4-(3-oxo-3-(piperazin-1-yl)prop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.000026
N-((E)-4-(3-oxo-3-(piperidin-4-ylamino)prop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.00032
N-(3,4-dimethoxyphenyl)-4-[2-(5-methyl-1H-imidazol-1-yl)ethyl]-1,3-thiazol-2-amine
Homo sapiens
pH 7.0, 37°C
0.00042
N-(3,4-dimethoxyphenyl)-5-[2-(5-methyl-1H-imidazol-1-yl)ethyl]-1,3,4-oxadiazol-2-amine
Homo sapiens
pH 7.0, 37°C
0.000029 - 0.0000292
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
0.0000264
N-(3-(2-(2-aminopyridin-4-yl)ethoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000079
N-(3-(2-aminoethoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.000015
N-(3-(3-(2-aminopyridin-4-yl)propoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.000009
N-(3-(3-aminopropoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000159
N-(3-(4-(2-aminopyridin-4-yl)butoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000468
N-(3-(4-(dimethylamino)butoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000088
N-(3-(4-aminobutoxy)-4-methoxyphenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000062
N-(3-methoxy-4-[[4-(piperidin-4-yl)phenyl]methoxy]phenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000162
N-(4-((1-(2-aminoethyl)piperidin-4-yl)carbamoyl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000565
N-(4-(2-(((2-aminopyridin-4-yl)methyl)amino)-2-oxoethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000079
N-(4-(2-((1-(2-aminoethyl)piperidin-4-yl)amino)-2-oxoethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000187
N-(4-(2-(piperazin-1-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000114
N-(4-(2-oxo-2-(piperazin-1-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000129
N-(4-(2-oxo-2-(piperidin-4-ylamino)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000247
N-(4-(4-(2-aminopyridin-4-yl)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000206
N-(4-methoxy-3-(2-(1-methylpiperidin-4-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000184
N-(4-methoxy-3-(2-(piperazin-1-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000073
N-(4-methoxy-3-(2-(piperidin-4-yl)ethoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000268
N-(4-methoxy-3-(3-(methylamino)propoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000158
N-(4-methoxy-3-(3-(piperazin-1-yl)propoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000088
N-(4-methoxy-3-(3-(piperidin-4-yl)propoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.000022
N-(4-methoxy-3-(4-(methylamino)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.000015
N-(4-methoxy-3-(4-(piperazin-1-yl)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000079
N-(4-methoxy-3-(4-(piperidin-4-yl)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000152
N-(4-methoxy-3-(4-(pyrimidin-2-ylamino)butoxy)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000112
N-(E)-(4-(3-(4-(2-aminoethyl)piperazin-1-yl)-3-oxoprop-1-en-1-yl)phenyl)-N'-(3-(5-methyl-1H-imidazol-1-yl)propyl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.0000088
N-[3-(4-aminobutoxy)-4-methoxyphenyl]-N'-[3-(2-methyl-1H-imidazol-1-yl)propyl]thiourea
Homo sapiens
pH and temperature not specified in the publication
0.00045
N2-[(2S)-1-hydroxy-2-[[3-(5-methyl-1H-imidazol-1-yl)propyl]amino]-3-phenylpropyl]-L-alaninamide
Homo sapiens
pH 7.0, 37°C
0.0053
PBD150
Homo sapiens
pH and temperature not specified in the publication
0.0000247
PQ912
Homo sapiens
pH 8.0, 25°C
0.000053
SEN-177
Homo sapiens
pH and temperature not specified in the publication
0.00017
SEN-180
Homo sapiens
pH and temperature not specified in the publication
0.0018
SEN-817
Homo sapiens
pH and temperature not specified in the publication
0.000013 - 0.00005
SEN177
0.000058
Sen180
Homo sapiens
pH and temperature not specified in the publication
0.0023
Sen817
Homo sapiens
pH and temperature not specified in the publication
0.000029
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
Homo sapiens
pH 7.0, 37°C
0.0000292
N-(3,4-dimethoxyphenyl)-N'-[3-(5-methyl-1H-imidazol-1-yl)propyl]thiourea
Homo sapiens
pH and temperature not specified in the publication
0.000013
SEN177
Homo sapiens
pH and temperature not specified in the publication
0.00005
SEN177
Homo sapiens
pH 8.0, 25°C, with enzyme mutant Y115E/Y117E
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evolution
glutaminyl cyclase (QC) and isoglutaminyl cyclase (isoQC) belong to the family of the metalloenzymes
evolution
glutaminyl cyclase (QC, glutaminyl-peptide cyclotransferase (QPCT)) and its isoenzyme isoQC (QPCTL) belong to a family of enzymes which catalyze the formation of pyroglutamate (pGlu, pE) at N-terminus of proteins by converting glutamate/glutamine to pGlu residue
evolution
glutaminyl cyclases (QCs) belong to the class of acyl transferases. Different types of QCs are identified in bacteria, plants and animals, including mammalian tissues
malfunction
knockdown of enzyme-transcript results in lower enzymatic activity, and small, unviable egg masses
malfunction
knockdown of enzyme-transcript results in lower enzymatic activity, and small, unviable egg masses
malfunction
glutaminyl cyclase inhibitors alter the CD47 protein by inhibiting QPCTL function and the resulting block in pGlu-modified CD47 is nearly complete. The expansion, differentiation, cytokine production and killing capacity of human T cells is compatible with small molecule inhibition of QPCTL. But QPCTL deficiency and QPCTL inhibition enhance tumor cell control by tumor-specific antibodies
malfunction
knockout of isoQC dramatically reduces the binding of SIRPalpha to cell surface
malfunction
loss of the pE-modification and N-terminal charge leads to accelerated aggregation of Abeta3(pE) compared with unmodified Abeta
metabolism
evidence for an involvement of glutaminyl cyclase (QC) in Alzheimer's disease pathogenesis via QC-catalyzed pE-Abeta formation
metabolism
the activity of myeloid cells such as macrophages and neutrophils is likewise regulated by a balance between stimulatory and inhibitory signals. In particular, cell surface expression of the CD47 protein creates a 'don't eat me' signal on tumor cells by binding to SIRPalpha expressed on myeloid cells. CD47 is a broadly expressed inhibitory ligand for myeloid cells. The glutaminyl-peptide cyclotransferase-like protein (QPCTL) is a major component of the CD47-SIRPalpha checkpoint. Interference with QPCTL expression leads to a major increase in neutrophil-mediated killing of tumor cells in vivo. Diglutamate formation occurs early in the CD47 protein life cycle and fully depends on QPCTL. Synergy between blockade of CD47 diglutamate formation and tumor opsonization in tumor cell killing by macrophages and neutrophils
metabolism
the dipeptidyl-peptidase activity of meprin beta links N-truncation of Abeta with glutaminyl cyclase-catalyzed pGlu-Abeta formation
metabolism
transmembrane protein CD47 is highly expressed on many types of cancer cells and can directly bind to the receptor signal regulatory protein alpha (SIRPalpha), which is highly expressed on phagocytic cells. Binding of CD47 to SIRPalpha can protect cancer cells from phagocytosis by phagocytic cells and therefore functions as the major 'don't eat me' signal. Therapeutic blockade of CD47-SIRPalpha axis can efficiently promote the macrophage-mediated phagocytosis and elimination of cancer cells. Glutaminyl cyclase isoenzyme isoQC is a regulator of SIRPalpha-CD47 axis
physiological function
-
glutaminyl cyclase contributes to the formation of focal and diffuse diglutamate-Abeta peptide deposits in hippocampus
physiological function
-
glutaminyl cyclase contributes to the formation of focal and diffuse diglutamate-Abeta peptide deposits in hippocampus
physiological function
amyloid-beta peptide Abeta3-40/42 is the precursor of pGlu-Abeta3-40/42 generated by glutaminyl cyclase (QC). The formation of amyloid-beta (Abeta) peptides is causally involved in the development of Alzheimer's disease (AD)
physiological function
diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxin peptide sequences and classification, overview
physiological function
diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview
physiological function
diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview
physiological function
diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview
physiological function
diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview
physiological function
diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview
physiological function
glutaminyl cyclase (QC) and isoglutaminyl cyclase (isoQC) catalyze the intramolecular cyclization of N-terminal L-glutamine/glutamate residues of certain proteins into diglutamic acid (pGlu). The amyloid protein and the monocyte chemoattractant protein (MCP-1) also known as CCL2 that promotes a cascade of inflammation-related responses are two representative substrates. The diglutamated Abeta and CCL2 exhibit more severe neurotoxicity than normal Abeta and CCL2. The Abeta1-40/42 peptides start with an L-aspartate at the N-terminus. Under pathological conditions, the Abeta1-40/42 peptides are truncated to expose the glutamate at position 3 or 11 of the Abeta peptides. Then the N-terminal glutamate (E) will be cyclized by QC to form the pyroglutamate (pE) and the products are termed as Abeta3(pE)-40/42 or Abeta11(pE)-40/42. The pE-modification of Abeta confers unique properties, such as proteolytic resistance. pGlu-Abeta peptides exhibit enhanced toxicity compared to the unmodified Abeta peptide and promote the formation of tau tangles. In Alzheimer's disease (AD) patients and animal AD models, the level and activity of QC are significantly increased
physiological function
glutaminyl cyclase (QC) and isoglutaminyl cyclase (isoQC) catalyze the intramolecular cyclization of N-terminal L-glutamine/glutamate residues of certain proteins into diglutamic acid (pGlu). The level of CCL2 and h-isoQCmRNA in Alzheimer disease (AD) patients is significantly higher than that of healthy subjects
physiological function
glutaminyl cyclase (QC) is one kind of acyltransferases, which catalyzes intramolecular cyclization of N-terminal glutamine residues to diglutamic acid (pGlu) with the concomitant liberation of ammonia. The post-translational formation of pGlu is an important process for the maturation of various bioactive neuropeptides, hormones, cytokines and for their biological activity, because the pGlu is required to protect the N termini from exopeptidase degradation and/or to develop the proper conformation. QC is abundant in mammalian secretory tissue such as secretory glands or brain tissue including hippocampus and cortex. Glutaminyl cyclase (QC) plays an important role in the initiation of the formation of neurotoxic plaques and in the pathogenesis of Alzheimer's disease (AD) due to the ability of human QC (hQC) to convert the N-terminal glutamate of beta-amyloids (Abetas) into respective pGlu-modified Abetas (pE-Abetas)
physiological function
glutaminyl cyclase activity correlates with levels of Abeta38, Abeta40 and angiogenesis mediators Flt1, Tie2, VEGFD, CAM-1 and ICAM-1 in cerebrospinal fluid of Alzheimers disease patients, core CSF diagnostic biomarkers (Abeta42, tau and p-tau) are not part of the diagnostic workup, detailed overview. Pyroglutamylation of truncated Abeta peptides, which is catalysed by enzyme glutaminyl cyclase (QC), generates pE-Abeta species with enhanced aggregation propensities and resistance to most amino-peptidases and endo-peptidases. pE-Abeta species have been identified as major constituents of Abeta plaques and reduction of pE-Abeta species is associated with improvement of cognitive tasks in animal models of Alzheimer's disease (AD). Some inflammatory or angiogenesis mediators are potential QC substrates
physiological function
glutaminyl cyclase isoenzyme isoQC is an essential regulator of CD47-SIRPalpha axis and required for efficient phagocytic cells-mediated clearance of cancer cells. N-terminal pGlu modification of proteins may protect protein from degradation by proteases or promote protein aggregation
physiological function
-
glutaminyl cyclase synthesized by Porphyromonas gingivalis (PgQC) is a key pathogen in developing periodontitis, potential link of periodontitis with rheumatoid arthritis (RA)
physiological function
glutaminyl cyclases (QCs) catalyze the intramolecular cyclization of N-terminal L-glutamine residues of peptides and proteins into pyroglutamic acid (5-oxo-prolyl, pGlu, pE) releasing ammonia, as well as the intramolecular cyclization of N-terminal glutamate residues into pyroglutamic acid. Such a type of post-translational modification stabilizes the peptides and proteins, protects them from proteolytic degradation, and can be important for their biological activity
physiological function
human glutaminyl cyclase (hQC) is an important enzyme for post-translational modification by converting the N-terminal glutaminyl and glutamyl into diglutamate (pGlu) through cyclization. The two isoforms of hQC, secretory glutaminyl cyclase (sQC) and Golgi resident glutaminyl cyclase (gQC), are involved in various pathological conditions especially in Alzheimer's disease (AD). The sQC is known to mediate the formation of diglutamate containing amyloid beta (pGlu-Abeta) peptides while gQC mediates the maturation of C-C motif chemokine ligand 2 (CCL2)
physiological function
the enzyme glutaminyl cyclase (QC) acts as glutamyl cyclase to catalyze pE-Abeta formation from N-terminal glutamate. A glutamate residue (E) is exposed at position 3 of Abeta(3-42) and can be converted by the enzymatic activity of glutaminyl cyclase (QC) to pE resulting in the peptide pE-Abeta(3-42). Slow conversion of N-terminal glutamate under slightly acidic pH conditions, as compared with the much faster pE formation from N-terminal glutamine
physiological function
the glutaminyl-peptide cyclotransferase-like protein (QPCTL) is a Golgi-resident enzyme that, like its secreted family member QPCT, can catalyze the cyclization of N-terminal glutamine and glutamic acid residues on target proteins into an N-terminal pyroglutamate residue (pGlu). QPCTL is a major component of the CD47-SIRPalpha checkpoint. Diglutamate formation occurs early in the CD47 protein life cycle and fully depends on QPCTL. QPCTL is critical for diglutamate formation on CD47 at the SIRPalpha binding site shortly after biosynthesis. QPCTL is a modulator of CD47-SIRPalpha binding. Genetic and pharmacological interference with QPCTL activity enhances antibody-dependent cellular phagocytosis and cellular cytotoxicity of tumor cells. Interference with QPCTL expression leads to a major increase in neutrophil-mediated killing of tumor cells in vivo
additional information
active site structure of gQC, residue W231 in gQC has adopted an outward positioning of the indole ring and is involved in hydrogen bonding with one of the neighboring amino acid P256. Substrate binding and structural analysis, detailed overview. In both QC isozymes, three acidic residues (E201, D248, and D305 in sQC, and E225, D269 and D326 in gQC) are pointed to each other and are likely to form hydrogen bonds between them. These residues play a major role in the catalysis. Catalytic reaction mechanism
additional information
active site structure of gQC, residue W231 in gQC has adopted an outward positioning of the indole ring and is involved in hydrogen bonding with one of the neighboring amino acid P256. Substrate binding and structural analysis, detailed overview. In both QC isozymes, three acidic residues (E201, D248, and D305 in sQC, and E225, D269 and D326 in gQC) are pointed to each other and are likely to form hydrogen bonds between them. These residues play a major role in the catalysis. Catalytic reaction mechanism
additional information
-
active site structure of gQC, residue W231 in gQC has adopted an outward positioning of the indole ring and is involved in hydrogen bonding with one of the neighboring amino acid P256. Substrate binding and structural analysis, detailed overview. In both QC isozymes, three acidic residues (E201, D248, and D305 in sQC, and E225, D269 and D326 in gQC) are pointed to each other and are likely to form hydrogen bonds between them. These residues play a major role in the catalysis. Catalytic reaction mechanism
additional information
-
enzyme expression analysis in Porphyromonas gingivalis on patients with chronic periodontitis (CP) and rheumatoid arthritis (RA), overview
additional information
two active site conformations are reported for sQC (Conf-A and Conf-B) and these are mainly associated with the orientation of W207. In Conf-A (open), the orientation of the indole ring of W207 is towards the surface of the molecule and in Conf-B (closed), the orientation is towards the Zn2+ ion. Substrate binding and structural analysis, detailed overview. In both QC isozymes, three acidic residues (E201, D248, and D305 in sQC, and E225, D269 and D326 in gQC) are pointed to each other and are likely to form hydrogen bonds between them. These residues play a major role in the catalysis. Residues C139 and C164 are not involved in catalysis. Catalytic reaction mechanism
additional information
two active site conformations are reported for sQC (Conf-A and Conf-B) and these are mainly associated with the orientation of W207. In Conf-A (open), the orientation of the indole ring of W207 is towards the surface of the molecule and in Conf-B (closed), the orientation is towards the Zn2+ ion. Substrate binding and structural analysis, detailed overview. In both QC isozymes, three acidic residues (E201, D248, and D305 in sQC, and E225, D269 and D326 in gQC) are pointed to each other and are likely to form hydrogen bonds between them. These residues play a major role in the catalysis. Residues C139 and C164 are not involved in catalysis. Catalytic reaction mechanism
additional information
-
two active site conformations are reported for sQC (Conf-A and Conf-B) and these are mainly associated with the orientation of W207. In Conf-A (open), the orientation of the indole ring of W207 is towards the surface of the molecule and in Conf-B (closed), the orientation is towards the Zn2+ ion. Substrate binding and structural analysis, detailed overview. In both QC isozymes, three acidic residues (E201, D248, and D305 in sQC, and E225, D269 and D326 in gQC) are pointed to each other and are likely to form hydrogen bonds between them. These residues play a major role in the catalysis. Residues C139 and C164 are not involved in catalysis. Catalytic reaction mechanism
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Busby, W.H.; Quackenbush, G.E.; Humm, J.; Youngblood, W.W.; Kizer, J.S.
An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes
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262
8532-8536
1987
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
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Fischer, W.H.; Spiess, J.
Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides
Proc. Natl. Acad. Sci. USA
84
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1987
Bos taurus, Rattus norvegicus
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Oberg, K.A.; Ruysschaert, J.M.; Azarkan, M.; Smolders, N.; Zerhouni, S.; Wintjens, R.; Amrani, A.; Looze, Y.
Papaya glutamine cyclase, a plant enzyme highly resistant to proteolysis, adopts an all-b conformation
Eur. J. Biochem.
258
214-222
1998
Carica papaya
brenda
Sykes, P.A.; Watson, S.J.; Temple, J.S.; Bateman, R.C., Jr.
Evidence for tissue-specific forms of glutaminyl cyclase
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455
159-161
1999
Bos taurus
brenda
Gololobov, M.Y.; Song, I.; Wang, W.; Bateman, R.C.M.
Steady-state kinetics of glutamine cyclotransferase
Arch. Biochem. Biophys.
309
300-307
1994
Carica papaya
brenda
Dahl, S.W.; Slaughter, C.; Lauritzen, C.; Bateman, R.C., Jr.; Connerton, I.; Pedersen, J.
Carica papaya glutamine cyclotransferase belongs to a novel plant enzyme subfamily: cloning and characterization of the recombinant Enzyme
Protein Expr. Purif.
20
27-36
2000
Carica papaya (O81226), Carica papaya
brenda
Gololobov, M.Y.; Wang, W.; Bateman, R.C., Jr.
Substrate and inhibitor specificity of glutamine cyclotransferase (QC)
Biol. Chem. Hoppe-Seyler
377
395-398
1996
Carica papaya
brenda
Song, I.; Chuang, C.Z.; Bateman, J.R.C.
Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase
J. Mol. Endocrinol.
13
77-86
1994
Homo sapiens
brenda
Bateman, R.C., Jr.; Temple, J.S.; Misquitta, S.A.; Booth, R.E.
Evidence for essential histidines in human pituitary glutaminyl cyclase
Biochemistry
40
11246-11250
2001
Homo sapiens
brenda
Schilling, S.; Hoffmann, T.; Rosche, F.; Manhart, S.; Wasternack, C.; Demuth, H.U.
Heterologous expression and characterization of human glutaminyl cyclase: evidence for a disulfide bond with importance for catalytic activity
Biochemistry
41
10849-10857
2002
Homo sapiens
brenda
Zerhouni, S.; Amrani, A.; Nijs, M.; Vandermeers, A.; Looze, Y.
Purification and characterization of the plant glutaminyl-peptide cyclotransferase isolated from papaya latex
Int. J. Bio-Chromatogr.
3
189-206
1997
Carica papaya
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brenda
Azarkan, M.; Amrani, A.; Zerhouni, S.; Oberg, K.A.; Ruysschaert, J.M.; Wintjens, R.; Looze, Y.
Evidence that thermodynamic stability of papaya glutamine cyclase is only marginal
Biopolymers
65
325-335
2002
Carica papaya
brenda
Azarkan, M.; Clantin, B.; Bompard, C.; Belrhali, H.; Baeyens-Volant, D.; Looze, Y.; Villeret, V.; Wintjens, R.
Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex
Acta Crystallogr. Sect. F
F61
59-61
2005
Carica papaya
brenda
Schilling, S.; Manhart, S.; Hoffmann, T.; Ludwig, H.H.; Wasternack, C.; Demuth, H.U.
Substrate specificity of glutaminyl cyclases from plants and animals
Biol. Chem.
384
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2003
Carica papaya, Homo sapiens
brenda
Booth, R.E.; Lovell, S.C.; Misquitta, S.A.; Bateman, R.C., Jr.
Human glutaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active site
BMC Biol.
2
2
2004
Homo sapiens (Q16769), Homo sapiens
brenda
Schilling, S.; Hoffmann, T.; Manhart, S.; Hoffmann, M.; Demuth, H.U.
Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions
FEBS Lett.
563
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2004
Carica papaya, Homo sapiens
brenda
Schilling, S.; Niestroj, A.J.; Rahfeld, J.U.; Hoffmann, T.; Wermann, M.; Zunkel, K.; Wasternack, C.; Demuth, H.U.
Identification of human glutaminyl cyclase as a metalloenzyme. Potent inhibition by imidazole derivatives and heterocyclic chelators
J. Biol. Chem.
278
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2003
Homo sapiens (Q16769), Homo sapiens
brenda
Huang, K.F.; Liu, Y.L.; Cheng, W.J.; Ko, T.P.; Wang, A.H.
Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation
Proc. Natl. Acad. Sci. USA
102
13117-13122
2005
Homo sapiens (Q16769), Homo sapiens
brenda
Booth, R.E.; Misquitta, S.A.; Bateman, R.C., Jr.
Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification
Protein Expr. Purif.
32
141-146
2003
Bos taurus, Homo sapiens
brenda
Huang, K.F.; Liu, Y.L.; Wang, A.H.
Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: a single zinc metalloenzyme
Protein Expr. Purif.
43
65-72
2005
Homo sapiens
brenda
Schilling, S.; Cynis, H.; von Bohlen, A.; Hoffmann, T.; Wermann, M.; Heiser, U.; Buchholz, M.; Zunkel, K.; Demuth, H.U.
Isolation, catalytic properties, and competitive inhibitors of the zinc-dependent murine glutaminyl cyclase
Biochemistry
44
13415-13424
2005
Mus musculus (Q9CYK2), Mus musculus
brenda
Cynis, H.; Schilling, S.; Bodnar, M.; Hoffmann, T.; Heiser, U.; Saido, T.C.; Demuth, H.
Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells
Biochim. Biophys. Acta
1764
1618-1625
2006
Homo sapiens, Mus musculus
brenda
Guevara, T.; Mallorqui-Fernandez, N.; Garcia-Castellanos, R.; Garcia-Pique, S.; Ebert Petersen, G.; Lauritzen, C.; Pedersen, J.; Arnau, J.; Gomis-Rueth, F.X.; Sola, M.
Papaya glutamine cyclotransferase shows a singular five-fold beta-propeller architecture that suggests a novel reaction mechanism
Biol. Chem.
387
1479-1486
2006
Carica papaya (O81226), Carica papaya
brenda
Schilling, S.; Stenzel, I.; von Bohlen, A.; Wermann, M.; Schulz, K.; Demuth, H.U.; Wasternack, C.
Isolation and characterization of the glutaminyl cyclases from Solanum tuberosum and Arabidopsis thaliana: implications for physiological functions
Biol. Chem.
388
145-153
2007
Arabidopsis thaliana, Solanum tuberosum, Solanum tuberosum (M1AKD0)
brenda
Buchholz, M.; Heiser, U.; Schilling, S.; Niestroj, A.J.; Zunkel, K.; Demuth, H.U.
The first potent inhibitors for human glutaminyl cyclase: synthesis and structure-activity relationship
J. Med. Chem.
49
664-677
2006
Homo sapiens
brenda
Wintjens, R.; Belrhali, H.; Clantin, B.; Azarkan, M.; Bompard, C.; Baeyens-Volant, D.; Looze, Y.; Villeret, V.
Crystal structure of papaya glutaminyl cyclase, an archetype for plant and bacterial glutaminyl cyclases
J. Mol. Biol.
357
457-470
2006
Carica papaya (O81226), Carica papaya
brenda
Pawlak, J.; Manjunatha Kini, R.
Snake venom glutaminyl cyclase
Toxicon
48
278-286
2006
Boiga irregularis (A7ISW1), Boiga irregularis, Boiga dendrophila (A7ISW2), Boiga dendrophila
brenda
Huang, K.F.; Wang, Y.R.; Chang, E.C.; Chou, T.L.; Wang, A.H.
A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis
Biochem. J.
411
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2008
Homo sapiens
brenda
Schilling, S.; Lindner, C.; Koch, B.; Wermann, M.; Rahfeld, J.U.; von Bohlen, A.; Rudolph, T.; Reuter, G.; Demuth, H.U.
Isolation and characterization of glutaminyl cyclases from Drosophila: evidence for enzyme forms with different subcellular localization
Biochemistry
46
10921-10930
2007
Drosophila melanogaster, Drosophila melanogaster (Q9VRQ9)
brenda
Cynis, H.; Scheel, E.; Saido, T.C.; Schilling, S.; Demuth, H.U.
Amyloidogenic processing of amyloid precursor protein: evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-beta
Biochemistry
47
7405-7413
2008
Homo sapiens
brenda
Gontsarova, A.; Kaufmann, E.; Tumani, H.; Dressel, A.; Mandel, F.; Wiesmueller, K.H.; Kunert-Keil, C.; Brinkmeier, H.
Glutaminyl cyclase activity is a characteristic feature of human cerebrospinal fluid
Clin. Chim. Acta
389
152-159
2008
Homo sapiens
brenda
Cynis, H.; Rahfeld, J.U.; Stephan, A.; Kehlen, A.; Koch, B.; Wermann, M.; Demuth, H.U.; Schilling, S.
Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery
J. Mol. Biol.
379
966-980
2008
Homo sapiens
brenda
Schilling, S.; Appl, T.; Hoffmann, T.; Cynis, H.; Schulz, K.; Jagla, W.; Friedrich, D.; Wermann, M.; Buchholz, M.; Heiser, U.; von Hoersten, S.; Demuth, H.U.
Inhibition of glutaminyl cyclase prevents pGlu-Abeta formation after intracortical/hippocampal microinjection in vivo/in situ
J. Neurochem.
106
1225-1236
2008
Rattus norvegicus
brenda
Schilling, S.; Zeitschel, U.; Hoffmann, T.; Heiser, U.; Francke, M.; Kehlen, A.; Holzer, M.; Hutter-Paier, B.; Prokesch, M.; Windisch, M.; Jagla, W.; Schlenzig, D.; Lindner, C.; Rudolph, T.; Reuter, G.; Cynis, H.; Montag, D.; Demuth, H.U.; Rossner, S.
Glutaminyl cyclase inhibition attenuates pyroglutamate Abeta and Alzheimers disease-like pathology
Nat. Med.
14
1106-1111
2008
Homo sapiens
brenda
Calvaresi, M.; Garavelli, M.; Bottoni, A.
Computational evidence for the catalytic mechanism of glutaminyl cyclase. A DFT investigation
Proteins
73
527-538
2008
Homo sapiens (Q16769)
brenda
Cornell, H.J.; Doherty, W.; Stelmasiak, T.
Papaya latex enzymes capable of detoxification of gliadin
Amino Acids
38
155-165
2009
Carica papaya, Carica papaya (O81226)
brenda
Seifert, F.; Schulz, K.; Koch, B.; Manhart, S.; Demuth, H.U.; Schilling, S.
Glutaminyl cyclases display significant catalytic proficiency for glutamyl substrates
Biochemistry
48
11831-11833
2009
Carica papaya, Homo sapiens, Mus musculus, Solanum tuberosum
brenda
Hook, V.; Schechter, I.; Demuth, H.U.; Hook, G.
Alternative pathways for production of beta-amyloid peptides of Alzheimers disease
Biol. Chem.
389
993-1006
2008
Rattus norvegicus
brenda
Stephan, A.; Wermann, M.; Von Bohlen, A.; Koch, B.; Cynis, H.; Demuth, H.; Schilling, S.
Mammalian glutaminyl cyclases and their isoenzymes have identical enzymatic characteristics
FEBS J.
276
6522-6536
2009
Homo sapiens, Mus musculus
brenda
Hartlage-Ruebsamen, M.; Staffa, K.; Waniek, A.; Wermann, M.; Hoffmann, T.; Cynis, H.; Schilling, S.; Demuth, H.U.; Rossner, S.
Developmental expression and subcellular localization of glutaminyl cyclase in mouse brain
Int. J. Dev. Neurosci.
27
825-835
2009
Mus musculus
brenda
Buchholz, M.; Hamann, A.; Aust, S.; Brandt, W.; Boehme, L.; Hoffmann, T.; Schilling, S.; Demuth, H.U.; Heiser, U.
Inhibitors for human glutaminyl cyclase by structure based design and bioisosteric replacement
J. Med. Chem.
52
7069-7080
2009
Homo sapiens (Q16769), Homo sapiens
brenda
Hartlage-Ruebsamen, M.; Morawski, M.; Waniek, A.; Jaeger, C.; Zeitschel, U.; Koch, B.; Cynis, H.; Schilling, S.; Schliebs, R.; Demuth, H.U.; Rossner, S.
Glutaminyl cyclase contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Abeta deposits in hippocampus via distinct cellular mechanisms
Acta Neuropathol.
121
705-719
2011
Homo sapiens, Mus musculus
brenda
Bowser, T.E.; Trawick, M.L.
Probing the specificity of gamma-glutamylamine cyclotransferase: an enzyme involved in the metabolism of transglutaminase-catalyzed protein crosslinks
Amino Acids
44
143-150
2013
Oryctolagus cuniculus
brenda
Ruiz-Carrillo, D.; Koch, B.; Parthier, C.; Wermann, M.; Dambe, T.; Buchholz, M.; Ludwig, H.H.; Heiser, U.; Rahfeld, J.U.; Stubbs, M.T.; Schilling, S.; Demuth, H.U.
Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center
Biochemistry
50
6280-6288
2011
Homo sapiens (Q16769), Mus musculus (Q9CYK2)
brenda
Koch, B.; Kolenko, P.; Buchholz, M.; Ruiz Carrillo, D.; Parthier, C.; Wermann, M.; Rahfeld, J.U.; Reuter, G.; Schilling, S.; Stubbs, M.T.; Demuth, H.U.
Crystal structures of glutaminyl cyclases (QCs) from Drosophila melanogaster reveal active site conservation between insect and mammalian QCs
Biochemistry
51
7383-7392
2012
Drosophila melanogaster (Q86PD7), Drosophila melanogaster (Q9VRQ9), Drosophila melanogaster
brenda
Carrillo, D.R.; Parthier, C.; Jaenckel, N.; Grandke, J.; Stelter, M.; Schilling, S.; Boehme, M.; Neumann, P.; Wolf, R.; Demuth, H.U.; Stubbs, M.T.; Rahfeld, J.U.
Kinetic and structural characterization of bacterial glutaminyl cyclases from Zymomonas mobilis and Myxococcus xanthus
Biol. Chem.
391
1419-1428
2010
Myxococcus xanthus (Q1DDS6), Zymomonas mobilis (Q5NLA9)
brenda
Koch, B.; Buchholz, M.; Wermann, M.; Heiser, U.; Schilling, S.; Demuth, H.U.
Probing secondary glutaminyl cyclase (QC) inhibitor interactions applying an in silico-modeling/site-directed mutagenesis approach: implications for drug development
Chem. Biol. Drug Des.
80
937-946
2012
Homo sapiens (Q16769), Mus musculus (Q9CYK2)
brenda
Huang, K.F.; Liaw, S.S.; Huang, W.L.; Chia, C.Y.; Lo, Y.C.; Chen, Y.L.; Wang, A.H.
Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding
J. Biol. Chem.
286
12439-12449
2011
Homo sapiens, Homo sapiens (Q9NXS2)
brenda
Huang, W.L.; Wang, Y.R.; Ko, T.P.; Chia, C.Y.; Huang, K.F.; Wang, A.H.
Crystal structure and functional analysis of the glutaminyl cyclase from Xanthomonas campestris
J. Mol. Biol.
401
374-388
2010
Xanthomonas campestris (Q8P8M4), Xanthomonas campestris, Xanthomonas campestris ATCC 33913 (Q8P8M4)
brenda
Huang, K.F.; Hsu, H.L.; Karim, S.; Wang, A.H.
Structural and functional analyses of a glutaminyl cyclase from Ixodes scapularis reveal metal-independent catalysis and inhibitor binding
Acta Crystallogr. Sect. D
70
789-801
2014
Ixodes scapularis (B7QK46), Ixodes scapularis
brenda
Waniek, A.; Hartlage-Ruebsamen, M.; Hoefling, C.; Kehlen, A.; Schilling, S.; Demuth, H.U.; Rossner, S.
Identification of thyrotropin-releasing hormone as hippocampal glutaminyl cyclase substrate in neurons and reactive astrocytes
Biochim. Biophys. Acta
1852
146-155
2015
Mus musculus
brenda
Becker, A.; Eichentopf, R.; Sedlmeier, R.; Waniek, A.; Cynis, H.; Koch, B.; Stephan, A.; Baeuscher, C.; Kohlmann, S.; Hoffmann, T.; Kehlen, A.; Berg, S.; Freyse, E.J.; Osmand, A.; Plank, A.C.; Rossner, S.; von Hoersten, S.; Graubner, S.; Demuth, H.U.; Schilling, S.
IsoQC (QPCTL) knock-out mice suggest differential substrate conversion by glutaminyl cyclase isoenzymes
Biol. Chem.
397
45-55
2016
Mus musculus
brenda
Seifert, F.; Demuth, H.U.; Weichler, T.; Ludwig, H.H.; Tittmann, K.; Schilling, S.
Phosphate ions and glutaminyl cyclases catalyze the cyclization of glutaminyl residues by facilitating synchronized proton transfers
Bioorg. Chem.
60
98-101
2015
Drosophila melanogaster
brenda
Adamson, S.W.; Browning, R.E.; Chao, C.C.; Bateman, R.C.; Ching, W.M.; Karim, S.
Molecular characterization of tick salivary gland glutaminyl cyclase
Insect Biochem. Mol. Biol.
43
781-793
2013
Ixodes scapularis (B7QK46), Ixodes scapularis, Amblyomma maculatum (G3MGU0)
brenda
Hoefling, C.; Indrischek, H.; Hoepcke, T.; Waniek, A.; Cynis, H.; Koch, B.; Schilling, S.; Morawski, M.; Demuth, H.U.; Rossner, S.; Hartlage-Ruebsamen, M.
Mouse strain and brain region-specific expression of the glutaminyl cyclases QC and isoQC
Int. J. Dev. Neurosci.
36
64-73
2014
Mus musculus
brenda
Cynis, H.; Funkelstein, L.; Toneff, T.; Mosier, C.; Ziegler, M.; Koch, B.; Demuth, H.U.; Hook, V.
Pyroglutamate-amyloid-beta and glutaminyl cyclase are colocalized with amyloid-beta in secretory vesicles and undergo activity-dependent, regulated secretion
Neurodegener. Dis.
14
85-97
2014
Bos taurus, Homo sapiens
brenda
Bridel, C.; Hoffmann, T.; Meyer, A.; Durieux, S.; Koel-Simmelink, M.A.; Orth, M.; Scheltens, P.; Lues, I.; Teunissen, C.E.
Glutaminyl cyclase activity correlates with levels of Abeta peptides and mediators of angiogenesis in cerebrospinal fluid of Alzheimers disease patients
Alzheimers Res. Ther.
9
38
2017
Homo sapiens (Q16769), Homo sapiens
brenda
Bender, P.; Egger, A.; Westermann, M.; Taudte, N.; Sculean, A.; Potempa, J.; Moeller, B.; Buchholz, M.; Eick, S.
Expression of human and Porphyromonas gingivalis glutaminyl cyclases in periodontitis and rheumatoid arthritis-A pilot study
Arch. Oral Biol.
97
223-230
2019
Porphyromonas gingivalis, Homo sapiens (Q16769), Homo sapiens (Q9NXS2), Homo sapiens
brenda
Li, M.; Dong, Y.; Yu, X.; Zou, Y.; Zheng, Y.; Bu, X.; Quan, J.; He, Z.; Wu, H.
Inhibitory effect of flavonoids on human glutaminyl cyclase
Bioorg. Med. Chem.
24
2280-2286
2016
Homo sapiens (Q16769), Homo sapiens
brenda
Ngo, V.T.H.; Hoang, V.H.; Tran, P.T.; Van Manh, N.; Ann, J.; Kim, E.; Cui, M.; Choi, S.; Lee, J.; Kim, H.; Ha, H.J.; Choi, K.; Kim, Y.H.; Lee, J.
Structure-activity relationship investigation of Phe-Arg mimetic region of human glutaminyl cyclase inhibitors
Bioorg. Med. Chem.
26
3133-3144
2018
Homo sapiens (Q16769), Homo sapiens
brenda
Wu, Z.; Weng, L.; Zhang, T.; Tian, H.; Fang, L.; Teng, H.; Zhang, W.; Gao, J.; Hao, Y.; Li, Y.; Zhou, H.; Wang, P.
Identification of glutaminyl cyclase isoenzyme isoQC as a regulator of SIRPalpha-CD47 axis
Cell Res.
29
502-505
2019
Homo sapiens (Q9NXS2)
brenda
Xu, A.; He, F.; Yu, C.; Qu, Y.; Zhang, Q.; Lv, J.; Zhang, X.; Ran, Y.; Wei, C.; Wu, J.
The development of small molecule inhibitors of glutaminyl cyclase and isoglutaminyl cyclase for Alzheimers disease
ChemistrySelect
4
10591-10600
2019
Homo sapiens (Q16769), Homo sapiens (Q9NXS2)
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brenda
Schlenzig, D.; Cynis, H.; Hartlage-Ruebsamen, M.; Zeitschel, U.; Menge, K.; Fothe, A.; Ramsbeck, D.; Spahn, C.; Wermann, M.; Rossner, S.; Buchholz, M.; Schilling, S.; Demuth, H.U.
Dipeptidyl-peptidase activity of meprin beta links N-truncation of Abeta with glutaminyl cyclase-catalyzed pGlu-Abeta formation
J. Alzheimers Dis.
66
359-375
2018
Homo sapiens (Q16769), Homo sapiens
brenda
Pozzi, C.; Di Pisa, F.; Benvenuti, M.; Mangani, S.
The structure of the human glutaminyl cyclase-SEN177 complex indicates routes for developing new potent inhibitors as possible agents for the treatment of neurological disorders
J. Biol. Inorg. Chem.
23
1219-1226
2018
Homo sapiens (Q16769), Homo sapiens (Q9NXS2), Homo sapiens
brenda
Vijayasarathy, M.; Basheer, S.M.; Balaram, P.
Cone snail glutaminyl cyclase sequences from transcriptomic analysis and mass spectrometric characterization of two pyroglutamyl conotoxins
J. Proteome Res.
17
2695-2703
2018
Conus monile (A0A2D1P879), Conus monile, Conus litteratus (A0A2D1P881), Conus litteratus, Conus amadis (A0A2D1P884), Conus amadis, Conus miles (A0A2D1P885), Conus miles, Conus frigidus (A0A2D1P886), Conus frigidus, Conus araneosus (A0A2D1P8A3)
brenda
Hielscher-Michael, S.; Griehl, C.; Buchholz, M.; Demuth, H.U.; Arnold, N.; Wessjohann, L.A.
Natural products from microalgae with potential against Alzheimers disease sulfolipids are potent glutaminyl cyclase inhibitors
Mar. Drugs
14
203
2016
Homo sapiens (Q16769)
brenda
Hartlage-Ruebsamen, M.; Bluhm, A.; Piechotta, A.; Linnert, M.; Rahfeld, J.U.; Demuth, H.U.; Lues, I.; Kuhn, P.H.; Lichtenthaler, S.F.; Rossner, S.; Hoefling, C.
Immunohistochemical evidence from APP-transgenic mice for glutaminyl cyclase as drug target to diminish pE-Abeta formation
Molecules
23
924
2018
Mus musculus (Q9CYK2)
brenda
Logtenberg, M.E.W.; Jansen, J.H.M.; Raaben, M.; Toebes, M.; Franke, K.; Brandsma, A.M.; Matlung, H.L.; Fauster, A.; Gomez-Eerland, R.; Bakker, N.A.M.; van der Schot, S.; Marijt, K.A.; Verdoes, M.; Haanen, J.B.A.G.; van den Berg, J.H.; Neefjes, J.; van den Berg, T.K.; Brummelkamp, T.R.; Leusen, J.H.W.; Scheeren, F.A.; Schumacher, T.N.
Glutaminyl cyclase is an enzymatic modifier of the CD47-SIRPalpha axis and a target for cancer immunotherapy
Nat. Med.
25
612-619
2019
Homo sapiens (Q9NXS2)
brenda
Vijayan, D.K.; Zhang, K.Y.J.
Human glutaminyl cyclase Structure, function, inhibitors and involvement in Alzheimers disease
Pharmacol. Res.
147
104342
2019
Homo sapiens (Q16769), Homo sapiens (Q9NXS2), Homo sapiens
brenda
Tran, P.; Hoang, V.; Lee, J.; Hien, T.; Tung, N.; Ngo, S.
In vitro and in silico determination of glutaminyl cyclase inhibitors
RSC Adv.
9
29619-29627
2019
Homo sapiens (Q16769)
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brenda