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Literature summary for 1.8.4.11 extracted from

  • Antoine, M.; Boschi-Muller, S.; Branlant, G.
    Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis (2003), J. Biol. Chem., 278, 45352-45357.
    View publication on PubMed
Search for more literature for 1.8.4.11

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant MsrAs in Escherichia coli strain BE002 Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
C198S site-directed mutagenesis, altered kinetics compared to the wild-type enzyme Neisseria meningitidis
C198S site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme Neisseria meningitidis
W35F site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme Neisseria meningitidis
W53F site-directed mutagenesis, altered kinetics compared to the wild-type enzyme Neisseria meningitidis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of disulfide formation in MsrA at Cys52/Cys198 at pH 5.5 and pH 8.0, 25°C, single turnover experiments, steady-state kinetics Neisseria meningitidis
additional information
-
 additional information detailed kinetics, wild-type and mutants MsrAs Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant MsrAs from Escherichia coli strain BE002 Neisseria meningitidis

Reaction

Reaction Comment Organism Reaction ID
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism of MsrA, the rate limiting step occurs after formation of the sulfenic acid intermediate and is associated with either the Cys51/Cys198 disulfide bond formation or the thioredoxin reduction process Neisseria meningitidis
a
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin catalytic mechanism, rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin and formation of the thiosulfenic acid intermediate on Cys51 Neisseria meningitidis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine (S)-sulfoxide + thioredoxin enzyme MsrA shows absolute specificity for the S-form of free methionine sulfoxide, no activity with the R-form, enzyme MsrA is oxidized at Cys51/Cys198 forming a disulfide Neisseria meningitidis L-methionine + thioredoxin disulfide + H2O
-
 ?
L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Neisseria meningitidis L-methionine + thioredoxin disulfide + H2O
-
 ?

Synonyms

Synonyms Comment Organism
methionine sulfoxide reductase A
-
 Neisseria meningitidis
MsrA
-
 Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Neisseria meningitidis
0.6
-
 L-methionine (S)-sulfoxide pH 5.5, 25°C, MsrA, steady-state conditions Neisseria meningitidis
7
-
 L-methionine (S)-sulfoxide pH 8.0, 25°C, MsrA, steady-state conditions Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Neisseria meningitidis
8
-
 L-methionine formation Neisseria meningitidis

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8
-
 Neisseria meningitidis

Cofactor

Cofactor Comment Organism Structure
thioredoxin
-
 Neisseria meningitidis
thioredoxin rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin in catalysis Neisseria meningitidis