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Literature summary extracted from

  • Weissbach, H.; Etienne, F.; Hoshi, T.; Heinemann, S.H.; Lowther, W.T.; Matthews, B.; St John, G.; Nathan, C.; Brot, N.
    Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function (2002), Arch. Biochem. Biophys., 397, 172-178.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.11 gene msrA Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 C52S site-directed mutagenesis, reduced activity compared to the wild-type, no complementation of a msrA knockout mutant Escherichia coli
1.8.4.11 additional information a knockout mutant shows reduced ability to attach to host lung and vein epithelial cells Streptococcus pneumoniae
1.8.4.11 additional information construction of knockout mutants which show higher sensitivity to hydrogen peroxide compared to wild-type cells which can be compensated by complementation with the wild-type msrA gene from either Escherichia coli or Mycobacterium tuberculosis, but a mutant C52S msrA gene cannot restore activity in the knockout mutant strain, mutants show reduced type 1 fimbriae-mediated mannose-dependent agglutination of erythrocytes Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.11 calmodulin-L-methionine (S)-sulfoxide + thioredoxin Escherichia coli
-
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Streptococcus pneumoniae
-
L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Escherichia coli substrates are several peptides and proteins, overview L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 additional information Escherichia coli the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function ?
-
?
1.8.4.11 additional information Streptococcus pneumoniae the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function ?
-
?
1.8.4.11 ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin Escherichia coli
-
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 calmodulin-L-methionine (R)-sulfoxide + thioredoxin Escherichia coli
-
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Escherichia coli substrates are peptides and proteins L-methionine + thioredoxin disulfide + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Escherichia coli
-
-
-
1.8.4.11 Streptococcus pneumoniae
-
-
-
1.8.4.12 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O reaction mechanism Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.4.12 additional information
-
in vivo MsrB activity is below detection limit Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 calmodulin-L-methionine (S)-sulfoxide + thioredoxin
-
Escherichia coli calmodulin-L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + 2 dithiothreitol
-
Escherichia coli L-methionine + dithiothreitol disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin
-
Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin
-
Streptococcus pneumoniae L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin substrates are several peptides and proteins, overview Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 additional information MsrA is specific for the S-form of the substrate Escherichia coli ?
-
?
1.8.4.11 additional information the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function Escherichia coli ?
-
?
1.8.4.11 additional information the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function Streptococcus pneumoniae ?
-
?
1.8.4.11 ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
-
Escherichia coli ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 calmodulin-L-methionine (R)-sulfoxide + thioredoxin
-
Escherichia coli calmodulin-L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + dithiothreitol
-
Escherichia coli L-methionine + dithiothreitol disulfide
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin
-
Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin substrates are peptides and proteins Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 additional information MsrB is specific for the R-form of the substrate Escherichia coli ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 MsrA
-
Escherichia coli
1.8.4.11 MsrA
-
Streptococcus pneumoniae
1.8.4.11 peptide methionine sulfoxide reductase
-
Escherichia coli
1.8.4.11 peptide methionine sulfoxide reductase
-
Streptococcus pneumoniae
1.8.4.12 MsrB
-
Escherichia coli
1.8.4.12 peptide methionine sulfoxide reductase
-
Escherichia coli
1.8.4.12 YeaA
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 dithiothreitol utilized in vitro Escherichia coli
1.8.4.11 thioredoxin physiologic cofactor Escherichia coli
1.8.4.12 dithiothreitol utilized in vitro Escherichia coli
1.8.4.12 thioredoxin physiologic cofactor Escherichia coli