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Literature summary extracted from

  • Kriznik, A.; Boschi-Muller, S.; Branlant, G.
    Kinetic evidence that methionine sulfoxide reductase A can reveal its oxidase activity in the presence of thioredoxin (2014), Arch. Biochem. Biophys., 548, 54-59 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 C86S/C206S KM and kcat value are 19fold higher and 40fold slower compared to wild type, respectively. The Cys198-Cys206 disulfide bond is rather reduced by thioredoxin under steady-state conditions instead of the Cys51-Cys198 disulfide bond Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.11 0.19
-
thioredoxin mutant C86S/C206S, pH 8.0, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Escherichia coli P0A744
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin
-
Escherichia coli acetyl-L-methionine-NHMe + thioredoxin disulfide + H2O
-
?
1.8.4.11 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 Escherichia coli ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.4.11 0.088
-
thioredoxin mutant C86S/C206S, pH 8.0, 25°C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 thioredoxin
-
Escherichia coli