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Literature summary for 1.8.4.12 extracted from

  • Neiers, F.; Sonkaria, S.; Olry, A.; Boschi-Muller, S.; Branlant, G.
    Characterization of the amino acids from Neisseria meningitidis methionine sulfoxide reductase B involved in the chemical catalysis and substrate specificity of the reductase step (2007), J. Biol. Chem., 282, 32397-32405.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Neisseria meningitidis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information reductase step kinetic parameters of the wild-type and mutated MsrB Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Neisseria meningitidis

Reaction

Reaction Comment Organism Reaction ID
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin formation of the MsrB substrate complex leads to an activation of the catalytic Cys-117 characterized by a decreased pKapp of about 2.7 pH units. The catalytic active MsrB form is the Cys117-/His103+ species with a pKapp of 6.6 and 8.3, respectively. His103 and to a lesser extent His100, Asn119, and Thr26 (via a water molecule) participate in the stabilization of the polarized form of the sulfoxide function and of the transition state. Trp65 is essential for the catalytic efficiency of the reductase step by optimizing the position of the substrate in the active site Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-L-methionine-(R)-S-oxide-NHMe + thioredoxin
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Neisseria meningitidis ?
-
?

Synonyms

Synonyms Comment Organism
methionine sulfoxide reductase B
-
Neisseria meningitidis
MsrB
-
Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information reductase step kinetic parameters of the wild-type and mutated MsrB Neisseria meningitidis