1.8.4.11: peptide-methionine (S)-S-oxide reductase
This is an abbreviated version!
For detailed information about peptide-methionine (S)-S-oxide reductase, go to the full flat file.
Reaction
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Synonyms
EC 1.8.4.6, ecdysone-induced protein 28/29 kDa, FMsr, LIC_10545, LIC_12978, linmsra1, linmsra2, LMJF_07_1140, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase, methionine sulfoxide reductase A, methionine sulfoxide reductases A, methionine sulfoxide-S-reductase, methionine sulphoxide reductase, methionine sulphoxide reductase A, methionine-S-sulfoxide reductase, MetSO-L12 reductase, More, mrsA, MSR, MSR10, MSR180, MsrA, MSRA-1, MsrA/B, MsrA/MsrB, MsrA1, MSRA2, MSRA4, msrAB, MsrABTk, MsrBA, Peptide Met(O) reductase, peptide methionine S-sulfoxide reductase, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase A, peptide methionine sulfoxide reductase type A, peptide methionine sulphoxide reductase, peptide-methionine (S)-S-oxide reductase, peptide-methionine sulfoxide reductase, PilA, PilB, PilB protein, PMSR, PMSRA, protein-methionine-S-oxide-reductase, sulindac reductase, TbmsrA, TCDM_14270
ECTree
Cofactor
Cofactor on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase
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dithiothreitol
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dithiothreitol
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absolutely dependent on in vitro and in vivo with substrate Hsp21
dithiothreitol
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MsrA can also utilize DTT as reductant, the membrane-isozyme shows only poor activity, while MsrA1 is not active with DTT
dithiothreitol
preferred cofactor in vitro
dithiothreitol
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utilized in vitro
NADPH
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NADPH
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membrane-bound enzyme form Mem-R,S-Msr
thioredoxin
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thioredoxin
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393073, 394092, 394096, 394098, 394104, 657734, 657754, 658213, 658214, 658217, 667034, 668357
thioredoxin
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dependent on
thioredoxin
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preferred cofactor
thioredoxin
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physiological cofactor
thioredoxin
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physiological cofactor
thioredoxin
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physiological cofactor
thioredoxin
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physiological cofactor
thioredoxin
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physiologic cofactor
thioredoxin
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cytosolic thioredoxins 1 and 2 are involved in regulation of MsrA exression
thioredoxin
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rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin in catalysis
thioredoxin
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Clostridium MsrA is inefficiently reducible by thioredoxin
additional information
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DTT can partially substitute for thioredoxin in vitro, low activity
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additional information
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DTT can substitute for thioredoxin in vitro
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additional information
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DTT can substitute for thioredoxin in vitro
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additional information
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DTT can substitute for thioredoxin in vitro
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additional information
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no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
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