Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
ac-L-Lys-L-Asn-L-Met(O)-L-Asp-L-Lys-dinitrophenol + dithiothreitol
ac-L-Lys-L-Asn-L-Met-L-Asp-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
-
-
-
-
?
ac-L-Lys-L-Asp-L-Met(O)-L-Asn-L-Lys-dinitrophenol + dithiothreitol
ac-L-Lys-L-Asp-L-Met-L-Asn-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
-
-
-
-
?
ac-L-Lys-L-Asp-L-Met(O)-L-Asp-L-Lys-dinitrophenol + dithiothreitol
ac-L-Lys-L-Asp-L-Met-L-Asp-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
-
-
-
-
?
ac-L-Lys-L-Phe-L-Met(O)-L-Lys-L-Lys-dinitrophenol + dithiothreitol
ac-L-Lys-L-Phe-L-Met-L-Lys-L-Lys-dinitrophenol + dithiothreitol disulfide + H2O
-
-
-
-
?
acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin
?
-
-
-
-
?
acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin
acetyl-L-methionine-NHMe + thioredoxin disulfide + H2O
-
-
-
?
alpha-synuclein + dithiothreitol
?
-
alpha-synuclein is oxidized at both Met1 and Met5 but not at Met116 or Met127
-
-
?
alpha-synuclein + thioredoxin disulfide + H2O
?
-
Met1 and Met5 within alpha-synuclein are oxidized to (S)-methionine sulfoxide
-
-
?
alpha-synuclein-L-methionine (S)-S-oxide + thioredoxin
alpha-synuclein-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
alpha1-antitrypsin + thioredoxin disulfide + H2O
?
-
Met358 within alpha1-antitrypsin is oxidized to (S)-methionine sulfoxide
-
-
?
apolipoprotein A-I + dithiothreitol
?
-
the myristoylated enzyme reduces the methionine sulfoxides in apolipoprotein A-I four times faster than nonmyristoylated enzyme
-
-
?
calmodulin + thioredoxin disulfide + H2O
?
-
Met77 within calmodulin is oxidized to (S)-methionine sulfoxide
-
-
r
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
calmodulin-L-methionine (S)-S-oxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
MsrBA is able to completely reduce (i.e., repair) MetSO in the calcium regulatory protein calmodulin. The efficient repair is the coordinate activity of the two catalytic domains in the MsrBA fusion protein, which results in a 1 order of magnitude rate enhancement in comparison to those of the individual MsrA or MsrB enzyme alone
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (S)-sulfoxide + NADPH + H+
dabsyl-L-methionine + NADP+ + H2O
synthetic substrate, MsrA is absolutely specific for the S-form, 7fold lower activity with NADPH compared to DTT
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(S)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsylated L-methionine (S)-sulfoxide + thioredoxin
dabsylated L-methionine + thioredoxin disulfide + H2O
dimethylsulfide + thioredoxin disulfide + H2O
dimethylsulfoxide + thioredoxin
DL-methionine (S)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
-
enzyme MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
Gly-L-Met-Gly + dithiothreitol
?
-
-
-
-
?
His6-Ala-Ala-Gln-MetO-Ile + DTT
His6-Ala-Ala-Gln-Met-Ile + DTT disulfide + H2O
-
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (R,S)-sulfoxide + glutathione
L-methionine + GSSG + H2O
-
-
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
L-methionine (S)-sulfoxide + dithiothreitol
?
-
the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
-
-
?
L-methionine (S)-sulfoxide + glutaredoxin 2
L-methionine + glutaredoxin 2 disulfide + H2O
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine (S)-sulfoxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine-(S)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
stereospecific reduction, 9-fluorenylmethyl chloroformate-labeled substrate
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine-(S)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
L-Pro-L-Met-L-Ala-L-Ile-L-Lys-L-Lys + dithiothreitol
?
-
-
-
-
?
methionine sulfoxide in alkyl hydroperoxide reductase C + thioredoxin
methionine in alkyl hydroperoxide reductase C + thioredoxin disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
the membrane-associated isozyme reduces both R- and S-stereoisomer of methionine sulfoxide in proteins
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine (S)-sulfoxide methyl ester + thioredoxin
N-acetyl-L-methionine methyl ester + thioredoxin disulfide + H2O
-
enzyme MsrA
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine-(S)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
-
enzyme reduces L-methionine (S)-sulfoxide of the protein substrate
-
-
?
peptide-L-methionine (S)-S-oxide + mycothiol
peptide-L-methionine + mycothione + H2O
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
Met sulfoxide residues in Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
racemic (ethanesulfinyl)benzene + dithiothreitol
(ethylsulfanyl)benzene + [(R)-ethanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic (methanesulfinyl)benzene + dithiothreitol
(methylsulfanyl)benzene + [(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
racemic 1-(methanesulfinyl)-4-methylbenzene + dithiothreitol
1-methyl-4-(methylsulfanyl)benzene + 1-[(R)-methanesulfinyl]-4-methylbenzene + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 1-bromo-4-(methanesulfinyl)benzene + dithiothreitol
1-bromo-4-(methylsulfanyl)benzene + 1-bromo-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
racemic 1-fluoro-2-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-2-(methylsulfanyl)benzene + 1-fluoro-2-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
racemic 1-fluoro-3-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-3-(methylsulfanyl)benzene + 1-fluoro-3-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
racemic 1-fluoro-4-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-4-(methylsulfanyl)benzene + 1-fluoro-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
racemic 1-methyl-4-(methanesulfinyl)benzene + dithiothreitol
1-methyl-4-(methylsulfanyl)benzene + 1-methyl-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
racemic 2-(methanesulfinyl)aniline + dithiothreitol
2-(methylsulfanyl)aniline + 2-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
racemic 2-(methanesulfinyl)naphthalene + dithiothreitol
2-(methylsulfanyl)naphthalene + 2-[(R)-methanesulfinyl]naphthalene + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 2-(methanesulfinyl)phenol + dithiothreitol
2-(methylsulfanyl)phenol + 2-[(R)-methanesulfinyl]phenol + dithiothreitol disulfide + H2O
racemic 3-(methanesulfinyl)aniline + dithiothreitol
3-(methylsulfanyl)aniline + 3-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 4-(methanesulfinyl)benzaldehyde + dithiothreitol
4-(methylsulfanyl)benzaldehyde + 4-[(R)-methanesulfinyl]benzaldehyde + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic N-[2-(methanesulfinyl)phenyl]acetamide + dithiothreitol
N-[2-(methylsulfanyl)phenyl]acetamide + N-(2-[(R)-methanesulfinyl]phenyl)acetamide+ dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
S-methyl p-tolyl sulfoxide + thioredoxin A
1-methyl-4-(methylsulfanyl)benzene + thioredoxin A disulfide + H2O
-
-
-
?
S-methyl p-tolyl sulfoxide + thioredoxin C
1-methyl-4-(methylsulfanyl)benzene + thioredoxin C disulfide + H2O
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
additional information
?
-
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
-
FMsr is specific for the S-isomer
-
-
?
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
-
-
-
-
?
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
-
-
?
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
-
MsrA is specific for the S-form, recombinant human calmodulin, recombinant rat enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview
-
-
?
dabsyl-L-methionine (S)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
synthetic substrate, MsrA is absolutely specific for the S-form
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
?
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
?
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
synthetic substrate, MsrA is absolutely specific for the S-form
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
FMsr is specific for the S-isomer
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
synthetic substrate
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsylated L-methionine (S)-sulfoxide + thioredoxin
dabsylated L-methionine + thioredoxin disulfide + H2O
-
-
-
-
r
dabsylated L-methionine (S)-sulfoxide + thioredoxin
dabsylated L-methionine + thioredoxin disulfide + H2O
-
-
-
-
r
dimethylsulfide + thioredoxin disulfide + H2O
dimethylsulfoxide + thioredoxin
-
-
-
?
dimethylsulfide + thioredoxin disulfide + H2O
dimethylsulfoxide + thioredoxin
-
-
-
-
?
dimethylsulfide + thioredoxin disulfide + H2O
dimethylsulfoxide + thioredoxin
-
-
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Hsp21 contains 6 methionine residues at positions 49, 52, 55, 59, 62, and 67, about half of the residues are reduced by the enzyme probably due to its stereospecificity
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
-
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
the MsrA-domain of MsrABTk is strictly specific for the reduction of L-methionine (S)-sulfoxide
-
-
?
L-methionine (S)-sulfoxide + glutaredoxin 2
L-methionine + glutaredoxin 2 disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + glutaredoxin 2
L-methionine + glutaredoxin 2 disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of L-methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, there exist MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
oxidation of protein-bound methionine results in loss of protein function, but can be reversed by the enzyme activity reducing methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
absolute specificity for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme MsrA, absolute specificity for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrA activity of the tandem domains of PilB, the MsrA domain alone does very poorly utilize the R-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme MsrA shows absolute specificity for the S-form of free methionine sulfoxide, no activity with the R-form, enzyme MsrA is oxidized at Cys51/Cys198 forming a disulfide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA activity of the tandem domains of PilB, the MsrA domain alone does not utilize the R-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the 2 MsrA enzymes are absolutely specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
L-methionine (S)-sulfoxide is the specific substrate
-
-
?
L-methionine (S)-sulfoxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
L-methionine (S)-sulfoxide is the specific substrate
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
thioredoxin from Leptospira interrogans
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
thioredoxin from Leptospira interrogans
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, free methionine-(S)-S-oxide
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine-(S)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
L-methionine-(S)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
thioredoxin from Leptospira interrogans
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
thioredoxin from Leptospira interrogans
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
peptide-L-methionine (S)-S-oxide + mycothiol
peptide-L-methionine + mycothione + H2O
-
-
-
?
peptide-L-methionine (S)-S-oxide + mycothiol
peptide-L-methionine + mycothione + H2O
-
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
MsrA suppresses dopaminergic cell death and protein aggregation induced by the complex I inhibitor rotenone or mutant alpha-synuclein, but not by the proteasome inhibitor MG132. MsrA protects against Parkinson's disease-related stresses primarily via methionine sulfoxide repair rather than by scavenging reactive oxygen species
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrate is oxidized ribosomal L12 protein
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrate is oxidized ribosomal L12 protein
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in oxidized protein repair
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
hormonal regulation of MsrA is implicated in conferring protection against oxidative stress in the Drosophila. Cells that are able to express MsrA were twice as resistant to H2O2 in comparison with cells that are not able to express this gene
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrates are oxidized ribosomal L12 protein or oxidized Met-enkephalin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrates are oxidized ribosomal L12 protein or oxidized Met-enkephalin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, the enzyme is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized A-type potassium channel ShC/B whose activity strongly depends on the oxidative state of a methionine residue in the N-terminal part of the polypeptide
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
the enzyme protects the epidermis cells against irradiation and oxidative damages, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in repair of oxidized proteins by reducing oxidized methionine residues, which is required for resistance to hydrogen peroxide and other reactive oxygen species, and for adherence to host cell surfaces
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
physiological role, overview
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
racemic (methanesulfinyl)benzene + dithiothreitol
(methylsulfanyl)benzene + [(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic (methanesulfinyl)benzene + dithiothreitol
(methylsulfanyl)benzene + [(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic (methanesulfinyl)benzene + dithiothreitol
(methylsulfanyl)benzene + [(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-bromo-4-(methanesulfinyl)benzene + dithiothreitol
1-bromo-4-(methylsulfanyl)benzene + 1-bromo-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 1-bromo-4-(methanesulfinyl)benzene + dithiothreitol
1-bromo-4-(methylsulfanyl)benzene + 1-bromo-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-bromo-4-(methanesulfinyl)benzene + dithiothreitol
1-bromo-4-(methylsulfanyl)benzene + 1-bromo-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-fluoro-2-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-2-(methylsulfanyl)benzene + 1-fluoro-2-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-fluoro-2-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-2-(methylsulfanyl)benzene + 1-fluoro-2-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-fluoro-3-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-3-(methylsulfanyl)benzene + 1-fluoro-3-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-fluoro-3-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-3-(methylsulfanyl)benzene + 1-fluoro-3-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-fluoro-4-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-4-(methylsulfanyl)benzene + 1-fluoro-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 1-fluoro-4-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-4-(methylsulfanyl)benzene + 1-fluoro-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-fluoro-4-(methanesulfinyl)benzene + dithiothreitol
1-fluoro-4-(methylsulfanyl)benzene + 1-fluoro-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-methyl-4-(methanesulfinyl)benzene + dithiothreitol
1-methyl-4-(methylsulfanyl)benzene + 1-methyl-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 1-methyl-4-(methanesulfinyl)benzene + dithiothreitol
1-methyl-4-(methylsulfanyl)benzene + 1-methyl-4-[(R)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
-
-
-
?
racemic 2-(methanesulfinyl)aniline + dithiothreitol
2-(methylsulfanyl)aniline + 2-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 2-(methanesulfinyl)aniline + dithiothreitol
2-(methylsulfanyl)aniline + 2-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
-
-
-
?
racemic 2-(methanesulfinyl)aniline + dithiothreitol
2-(methylsulfanyl)aniline + 2-[(R)-methanesulfinyl]aniline + dithiothreitol disulfide + H2O
-
-
-
?
racemic 2-(methanesulfinyl)phenol + dithiothreitol
2-(methylsulfanyl)phenol + 2-[(R)-methanesulfinyl]phenol + dithiothreitol disulfide + H2O
-
specifically reduces the (S)-enantiomer of methionine sulfoxide to methionine
-
-
?
racemic 2-(methanesulfinyl)phenol + dithiothreitol
2-(methylsulfanyl)phenol + 2-[(R)-methanesulfinyl]phenol + dithiothreitol disulfide + H2O
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
highest activity by enzyme MsrA, low activity by enzyme MsrA1
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, mutation of gene msrA has no effect on virulence, and on resistance to oxidative agents, and causes no defect in cell envelope, msrA is probably linked to biofilm formation, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
?
additional information
?
-
the enzyme is not a major virulence determinant in the oral pathogen, MsrA is required for protein repair and protection against oxidative damage as well as for the proper expression or maintenance of functional adhesins
-
-
?
additional information
?
-
dunring the regeneration mechanism of MsrA by glutaredoxin, the catalytic Cys16 attacks the sulfoxide moiety of the substrate to form a sulfenic acid intermediate with the concomitant release of the product methionine. The catalytic Cys16 sulfenic acid is then attacked by glutaredoxin, leading to the formation of a complex through a mixed disulfide bond, which is reduced by glutathione, leading to MsrA regeneration
-
-
?
additional information
?
-
-
dunring the regeneration mechanism of MsrA by glutaredoxin, the catalytic Cys16 attacks the sulfoxide moiety of the substrate to form a sulfenic acid intermediate with the concomitant release of the product methionine. The catalytic Cys16 sulfenic acid is then attacked by glutaredoxin, leading to the formation of a complex through a mixed disulfide bond, which is reduced by glutathione, leading to MsrA regeneration
-
-
?
additional information
?
-
dunring the regeneration mechanism of MsrA by glutaredoxin, the catalytic Cys16 attacks the sulfoxide moiety of the substrate to form a sulfenic acid intermediate with the concomitant release of the product methionine. The catalytic Cys16 sulfenic acid is then attacked by glutaredoxin, leading to the formation of a complex through a mixed disulfide bond, which is reduced by glutathione, leading to MsrA regeneration
-
-
?
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
the reduction step is rate-determining
-
-
?
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA protects neuronal cells against brief hypoxia/reoxygenation, the enzyme is involved in oxidized protein repair and protects cells against reactive oxygen species and oxidative damage preventing apoptosis, overview
-
-
?
additional information
?
-
-
detoxification enzyme
-
-
?
additional information
?
-
enzyme converts free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme converts free and protein-bound methionine
-
-
?
additional information
?
-
MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways. Mrx1 reduces the sulfenic acid intermediate via the formation of an S-mycothiolated MsrA intermediate which is then recycled by mycoredoxin and a second molecule of mycothiol, similarly to the glutathione/glutaredoxin/glutathione reductase system. Trx reduces the Cys204-Cys213 disulfide bond in MsrA produced during methionine sulfoxide reduction via the formation of a transient intermolecular disulfide bond between Trx and MsrA
-
-
?
additional information
?
-
-
MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways. Mrx1 reduces the sulfenic acid intermediate via the formation of an S-mycothiolated MsrA intermediate which is then recycled by mycoredoxin and a second molecule of mycothiol, similarly to the glutathione/glutaredoxin/glutathione reductase system. Trx reduces the Cys204-Cys213 disulfide bond in MsrA produced during methionine sulfoxide reduction via the formation of a transient intermolecular disulfide bond between Trx and MsrA
-
-
?
additional information
?
-
MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways. Mrx1 reduces the sulfenic acid intermediate via the formation of an S-mycothiolated MsrA intermediate which is then recycled by mycoredoxin and a second molecule of mycothiol, similarly to the glutathione/glutaredoxin/glutathione reductase system. Trx reduces the Cys204-Cys213 disulfide bond in MsrA produced during methionine sulfoxide reduction via the formation of a transient intermolecular disulfide bond between Trx and MsrA
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
enzyme reduces oxidized methionine residues of the shaker potassium channel, which becomes reversibly inactivated upon oxidation
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
physiological role
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
?
additional information
?
-
-
MsrA is specific for the S-form of the substrate
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
?
additional information
?
-
-
substrate specificity of enzyme forms with S-form of free and protein-bound methionine sulfoxide, overview
-
-
?
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation
-
-
?
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates
-
-
?
additional information
?
-
-
the reduction step is rate-determining
-
-
?
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
?
additional information
?
-
enzyme catalyzes two reductase steps. In the presence of thioredoxin, the overall rate-limiting step is associated with the thioredoxin-recycling process, and MsrA accumulates under Cys51 sulfenic acid state. Formation of the second mol of Ac-L-Met-NHMe is rate-limiting in the absence of thioredoxin
-
-
?
additional information
?
-
-
enzyme catalyzes two reductase steps. In the presence of thioredoxin, the overall rate-limiting step is associated with the thioredoxin-recycling process, and MsrA accumulates under Cys51 sulfenic acid state. Formation of the second mol of Ac-L-Met-NHMe is rate-limiting in the absence of thioredoxin
-
-
?
additional information
?
-
MsrA oxidation mechanism follows three consecutive, pH dependent steps, corresponding to the oxidation of tyrosine, tryptophan and histidine amino acid residues
-
-
?
additional information
?
-
-
the enzyme fulfills both MetO reduction and protein deglutathionylation functions and is also capable of regenerating poplar peroxiredoxin IIB
-
-
?
additional information
?
-
-
the enzyme is unable to reduce insulin disulfides
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
the enzyme also exhibits MsrB activity utilizing L-methionine (R)-sulfoxide as substrate
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
downregulation of MsrA during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is an essential regulator of longevity and is important for lens cell viability and resistance to oxidative stress, methionine sulfoxide is the major oxidative stress product, up to 60%, in cataract while being essentially absent in clear lens
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
?
additional information
?
-
-
enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
-
-
?
additional information
?
-
-
identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
-
-
?
additional information
?
-
MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
-
-
?
additional information
?
-
-
MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
-
-
?
additional information
?
-
MsrA repairs methionine oxidized alpha-crystallin and restores the chaperone activity of alpha-crystallin lost upon methionine oxidation, Met-68 of alphabeta-crystallin is oxidized to protein methionine sulfoxide in the actual lens
-
-
?
additional information
?
-
-
the enzyme catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, MsrA can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells
-
-
?
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA is a regulator of antioxidant defense and lifespan in mammals
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
role of subcellular localization in structure-function relationship of the isozymes, overview
-
-
?
additional information
?
-
-
MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking
-
-
?
additional information
?
-
-
MsrA null mutant mice exhibit a shortened lifespan and present higher levels of protein carbonyls when exposed to hyperoxia, which indicates an increased sensitivity towards oxidative stress
-
-
?
additional information
?
-
the lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
-
-
?
additional information
?
-
MsrA repairs methionine oxidized alpha-crystallin and restores the chaperone activity of alpha-crystallin lost upon methionine oxidation, Met-68 of alphabeta-crystallin is oxidized to protein methionine sulfoxide in the actual lens
-
-
?
additional information
?
-
-
no oxidation or reduction of L-methionine in 14-3-3 zeta/delta protein, actin, alpha-crystallin A, alpha-crystallin B, apolipoprotein A, glutamine synthetase, peroxiredoxin 6, and thioredoxin
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
?
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
-
-
?
additional information
?
-
the tandem domains of PilB also posesses MsrB activity utilizing L-methionine (R)-sulfoxide as substrate, the MsrB domain alone does not utilize the S-isomer
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzymes acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
substrate specificities of enzymes, the reduction step is rate-determining
-
-
?
additional information
?
-
-
substrate specificity of MsrA activity, diverse substrates, overview
-
-
?
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
?
additional information
?
-
the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, enzyme activity is not age-related
-
-
?
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA protects the cell against damage caused by oxidative stress through treatment with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway
-
-
?
additional information
?
-
-
the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
-
-
?
additional information
?
-
MsrA utilizes two times more NADPH for the reduction of S-methyl p-tolyl sulfoxide when thioredoxin TrxA is included in the assays as compared to TrxC
-
-
?
additional information
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, MsrA is important for virulence in mice
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60%
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
no activity with glutathione
-
-
-
additional information
?
-
no activity with glutathione
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
the reduction step is rate-determining
-
-
?
additional information
?
-
the enzyme plays an important role in the oxidative stress response
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
L-methionine (S)-sulfoxide + dithiothreitol
?
-
the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
MsrA suppresses dopaminergic cell death and protein aggregation induced by the complex I inhibitor rotenone or mutant alpha-synuclein, but not by the proteasome inhibitor MG132. MsrA protects against Parkinson's disease-related stresses primarily via methionine sulfoxide repair rather than by scavenging reactive oxygen species
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
Met sulfoxide residues in Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
additional information
?
-
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
oxidation of protein-bound methionine results in loss of protein function, but can be reversed by the enzyme activity reducing methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in oxidized protein repair
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
hormonal regulation of MsrA is implicated in conferring protection against oxidative stress in the Drosophila. Cells that are able to express MsrA were twice as resistant to H2O2 in comparison with cells that are not able to express this gene
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, the enzyme is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized A-type potassium channel ShC/B whose activity strongly depends on the oxidative state of a methionine residue in the N-terminal part of the polypeptide
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
the enzyme protects the epidermis cells against irradiation and oxidative damages, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in repair of oxidized proteins by reducing oxidized methionine residues, which is required for resistance to hydrogen peroxide and other reactive oxygen species, and for adherence to host cell surfaces
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
physiological role, overview
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, mutation of gene msrA has no effect on virulence, and on resistance to oxidative agents, and causes no defect in cell envelope, msrA is probably linked to biofilm formation, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
?
additional information
?
-
the enzyme is not a major virulence determinant in the oral pathogen, MsrA is required for protein repair and protection against oxidative damage as well as for the proper expression or maintenance of functional adhesins
-
-
?
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA protects neuronal cells against brief hypoxia/reoxygenation, the enzyme is involved in oxidized protein repair and protects cells against reactive oxygen species and oxidative damage preventing apoptosis, overview
-
-
?
additional information
?
-
-
detoxification enzyme
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
physiological role
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
?
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
downregulation of MsrA during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is an essential regulator of longevity and is important for lens cell viability and resistance to oxidative stress, methionine sulfoxide is the major oxidative stress product, up to 60%, in cataract while being essentially absent in clear lens
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
-
-
?
additional information
?
-
-
identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
-
-
?
additional information
?
-
MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
-
-
?
additional information
?
-
-
MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
-
-
?
additional information
?
-
-
the enzyme catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, MsrA can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells
-
-
?
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA is a regulator of antioxidant defense and lifespan in mammals
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking
-
-
?
additional information
?
-
-
MsrA null mutant mice exhibit a shortened lifespan and present higher levels of protein carbonyls when exposed to hyperoxia, which indicates an increased sensitivity towards oxidative stress
-
-
?
additional information
?
-
the lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
?
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
enzymes acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, enzyme activity is not age-related
-
-
?
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA protects the cell against damage caused by oxidative stress through treatment with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway
-
-
?
additional information
?
-
-
the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
-
-
?
additional information
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, MsrA is important for virulence in mice
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60%
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
the enzyme plays an important role in the oxidative stress response
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.