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actin peptide H + S-adenosyl-L-methionine
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
synthetic peptide based on amino acid sequence of actin
-
?
S-adenosyl-L-methionine + 3-aminobutanoyl-His
S-adenosyl-L-homocysteine + 3-aminobutanoyl-Ntau-methyl-His
-
about 50% of the activity with carnosine
-
?
S-adenosyl-L-methionine + 3-aminobutanoyl-His
S-adenosyl-L-homocysteine + 3-aminobutanoyl-Ntau-methyl-L-His
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
S-adenosyl-L-methionine + Gly-Gly-His
S-adenosyl-L-homocysteine + Gly-Gly-Ntau-methyl-L-His
S-adenosyl-L-methionine + Gly-His
S-adenosyl-L-homocysteine + Gly-Ntau-methyl-L-His
S-adenosyl-L-methionine + homocarnosine
S-adenosyl-L-homocysteine + homoanserine
S-adenosyl-L-methionine + L-histidine
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
additional information
?
-
S-adenosyl-L-methionine + 3-aminobutanoyl-His
S-adenosyl-L-homocysteine + 3-aminobutanoyl-Ntau-methyl-L-His
-
about 50% of the activity with carnosine
-
?
S-adenosyl-L-methionine + 3-aminobutanoyl-His
S-adenosyl-L-homocysteine + 3-aminobutanoyl-Ntau-methyl-L-His
-
about 60% of the activity with carnosine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + Gly-Gly-His
S-adenosyl-L-homocysteine + Gly-Gly-Ntau-methyl-L-His
similar activity as with carnosine
-
-
?
S-adenosyl-L-methionine + Gly-Gly-His
S-adenosyl-L-homocysteine + Gly-Gly-Ntau-methyl-L-His
similar activity as with carnosine
-
-
?
S-adenosyl-L-methionine + Gly-Gly-His
S-adenosyl-L-homocysteine + Gly-Gly-Ntau-methyl-L-His
similar activity as with carnosine
-
-
?
S-adenosyl-L-methionine + Gly-His
S-adenosyl-L-homocysteine + Gly-Ntau-methyl-L-His
similar activity as with carnosine
-
-
?
S-adenosyl-L-methionine + Gly-His
S-adenosyl-L-homocysteine + Gly-Ntau-methyl-L-His
similar activity as with carnosine
-
-
?
S-adenosyl-L-methionine + Gly-His
S-adenosyl-L-homocysteine + Gly-Ntau-methyl-L-His
similar activity as with carnosine
-
-
?
S-adenosyl-L-methionine + homocarnosine
S-adenosyl-L-homocysteine + homoanserine
-
-
-
?
S-adenosyl-L-methionine + homocarnosine
S-adenosyl-L-homocysteine + homoanserine
-
-
-
?
S-adenosyl-L-methionine + L-histidine
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
-
-
-
?
S-adenosyl-L-methionine + L-histidine
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
-
-
-
?
S-adenosyl-L-methionine + L-histidine
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
-
-
-
?
additional information
?
-
very poor substrates: anserine, imidazole-4-acetic acid, imidazole-4-acrylic acid, L-histidine, histamine, imidazole
-
-
?
additional information
?
-
-
very poor substrates: anserine, imidazole-4-acetic acid, imidazole-4-acrylic acid, L-histidine, histamine, imidazole
-
-
?
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actin peptide H + S-adenosyl-L-methionine
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
synthetic peptide based on amino acid sequence of actin
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
-
-
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
-
biosynthesis of anserine
-
?
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C123A
mutation in disulfide bridge, displays strongly enhanced activity compared to that of wild-type
C238A
mutation in disulfide bridge, significantly reduces the activity
D278A/T279A
mutant barely displays any affinity to SAM
E167A
mutant barely displays any affinity to SAM
H309A
about 40% of wild-type activity
L307F
activity similar to wild-type
N274A
substantial reduction in expression level. Mutant barely displays any affinity to SAM
Q108A
mutant barely displays any affinity to SAM
R111A
mutant barely displays any affinity to SAM
S104A
activity similar to wild-type
S234A
mutant barely displays any affinity to SAM
Y286A
about 10fold lower affinity to SAM than wild-type
Y371A
substantial reduction in expression level, mutant barely displays any affinity to SAM
C123A
-
mutation in disulfide bridge, displays strongly enhanced activity compared to that of wild-type
-
E167A
-
mutant barely displays any affinity to SAM
-
H309A
-
about 40% of wild-type activity
-
R111A
-
mutant barely displays any affinity to SAM
-
S234A
-
mutant barely displays any affinity to SAM
-
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McManus, R.
Enzymatic synthesis of anserine in skeletal muscle by N-methylation of carnosine
J. Biol. Chem.
237
1207-1211
1962
Cavia porcellus, Gallus gallus, Oryctolagus cuniculus, Felis catus, Rattus norvegicus
-
brenda
Raghavan, M.; Lindberg, U.; Schutt, C.
The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymes
Eur. J. Biochem.
210
311-318
1992
Oryctolagus cuniculus
brenda
Drozak, J.; Piecuch, M.; Poleszak, O.; Kozlowski, P.; Chrobok, L.; Baelde, H.J.; de Heer, E.
UPF0586 protein C9orf41 homolog is anserine-producing methyltransferase
J. Biol. Chem.
290
17190-17205
2015
Gallus gallus (F1N9S8), Gallus gallus, Rattus norvegicus (Q5BJZ6), Homo sapiens (Q8N4J0), Homo sapiens
brenda
Drozak, J.; Chrobok, L.; Poleszak, O.; Jagielski, A.K.; Derlacz, R.
Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (HNMT-like)
PLoS ONE
8
e64805
2013
Gallus gallus (U3NEE3), Gallus gallus
brenda
Liu, X.; Wu, J.; Sun, Y.; Xie, W.
Substrate recognition mechanism of the putative yeast carnosine N-methyltransferase
ACS Chem. Biol.
12
2164-2171
2017
Saccharomyces cerevisiae (P53934), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P53934)
brenda