Literature summary for 1.8.4.11 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 .

Search for more literature for 1.8.4.11

Protein Variants

Protein Variants	Comment	Organism
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]

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A744	-	-

Substrates and Products (Substrate)

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

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

Cofactor

Cofactor	Comment	Organism	Structure
thioredoxin	-	Escherichia coli

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Release 2023.1 (January 2023)