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Literature summary extracted from

  • Olry, A.; Boschi-Muller, S.; Branlant, G.
    Kinetic characterization of the catalytic mechanism of methionine sulfoxide reductase B from Neisseria meningitidis (2004), Biochemistry, 43, 11616-11622.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.12 expression of wild-type and mutant enzymes in Escherichia coli Neisseria meningitidis

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.12 C63S site-directed mutagenesis, the mutant accumulates the sulfenic acid intermediate, while the wild-type accumulates the disulfide intermediate Neisseria meningitidis
1.8.4.12 W65F site-directed mutagenesis, structural change of substrate binding and active site structure compared to the wild-type enzyme Neisseria meningitidis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.12 additional information
-
additional information stopped flow kinetics, steady-state kinetics Neisseria meningitidis
1.8.4.12 0.026
-
thioredoxin pH 5.5, 25°C Neisseria meningitidis
1.8.4.12 0.14
-
acetyl-L-methionine (R)-sulfoxide N-methyl ester pH 5.5, 25°C Neisseria meningitidis
1.8.4.12 2.2
-
acetyl-L-methionine (R)-sulfoxide N-methyl ester pH 8.0, 25°C Neisseria meningitidis
1.8.4.12 7
-
thioredoxin pH 8.0, 25°C Neisseria meningitidis

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O three-step catalytic mechanism, influence of pH on reaction mechanism, overview Neisseria meningitidis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.12 acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin the affinity of MsrB to acetyl-L-methionine (R)-sulfoxide methyl ester is higher than to L-methionine (R)-sulfoxide Neisseria meningitidis L-methionine methyl ester + thioredoxin disulfide + H2O
-
?
1.8.4.12 acetyl-L-methionine (R)-sulfoxide N-methyl ester + thioredoxin
-
Neisseria meningitidis L-methionine methyl ester + thioredoxin disulfide + H2O
-
r
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB specifically reduces the R-form of methionine sulfoxide Neisseria meningitidis L-methionine + thioredoxin disulfide + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.8.4.12 monomer
-
Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
1.8.4.12 methionine sulfoxide reductase B
-
Neisseria meningitidis
1.8.4.12 MsrB
-
Neisseria meningitidis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.4.12 additional information
-
additional information
-
Neisseria meningitidis

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.12 thioredoxin dependent on Neisseria meningitidis