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Literature summary extracted from

  • Gand, A.; Antoine, M.; Boschi-Muller, S.; Branlant, G.
    Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase A (2007), J. Biol. Chem., 282, 20484-20491.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.11 additional information
-
 additional information steady-state and reductase step kinetic parameters of wild-type and mutated MsrAs Neisseria meningitidis

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Neisseria meningitidis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.11 peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin presence of at least two binding subsites. The first one, whose contribution is major in the efficiency of the reductase step and in which the epsilon-methyl group of MetSO binds, is the hydrophobic pocket formed by Phe52 and Trp53, the position of the indole ring being stabilized by interactions with His186 and Tyr189. The second subsite composed of Asp129 and Tyr197 contributes to the binding of the main chain of the substrate but to a lesser extent Neisseria meningitidis
a

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
-
 Neisseria meningitidis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 methionine sulfoxide reductase A
-
 Neisseria meningitidis
1.8.4.11 MsrA
-
 Neisseria meningitidis