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Literature summary extracted from

  • Spector, D.; Etienne, F.; Brot, N.; Weissbach, H.
    New membrane-associated and soluble peptide methionine sulfoxide reductases in Escherichia coli (2003), Biochem. Biophys. Res. Commun., 302, 284-289.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 additional information construction of a MsrA/MsrB double mutant Escherichia coli
1.8.4.12 additional information construction of a MsrA/MsrB double mutant Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.11 membrane membrane-associated isozyme, MsrA Escherichia coli 16020
-
1.8.4.11 soluble soluble isozyme MsrA1 Escherichia coli
-
-
1.8.4.12 membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.11 protein-L-methionine (S)-sulfoxide + thioredoxin Escherichia coli MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin protein-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 protein-L-methionine-(R)-sulfoxide + thioredoxin Escherichia coli MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin protein-L-methionine + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Escherichia coli
-
 wild-type strain MC1061, isozyme MsrA, a membrane-associated isozyme, and a soluble isozyme MsrA1
-
1.8.4.12 Escherichia coli
-
 wild-type strain MC1061, isozyme MsrB and a membrane-associated isozyme
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.4.11 0.0004
-
 membrane vesicles, substrate N-acetyl-L-methionine-(R)-sulfoxide Escherichia coli
1.8.4.11 0.00044
-
 MsrA, substrate N-acetyl-L-methionine-(S)-sulfoxide Escherichia coli
1.8.4.11 0.00047
-
 membrane vesicles, substrate N-acetyl-L-methionine-(S)-sulfoxide Escherichia coli
1.8.4.12 0.00022
-
 MsrB, substrate N-acetyl-L-methionine-(R)-sulfoxide Escherichia coli
1.8.4.12 0.0004
-
 membrane vesicles, substrate N-acetyl-L-methionine-(R)-sulfoxide Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 L-methionine (R)-sulfoxide + thioredoxin the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 additional information the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates Escherichia coli ?
-
 ?
1.8.4.11 N-acetyl-L-methionine (R)-sulfoxide + thioredoxin the membrane-associated isozyme reduces both R- and S-stereoisomer of methionine sulfoxide in proteins Escherichia coli N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 N-acetyl-L-methionine (S)-sulfoxide + thioredoxin MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers Escherichia coli N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 protein-L-methionine (S)-sulfoxide + thioredoxin MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin Escherichia coli protein-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 additional information the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates, the membrane-associated isozyme also shows MsrA activity utilizing L-methionine (S)-sulfoxide and N-acetyl-L-methionine (S)-sulfoxide as substrates Escherichia coli ?
-
 ?
1.8.4.12 N-acetyl-L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers Escherichia coli N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 protein-L-methionine-(R)-sulfoxide + thioredoxin MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin Escherichia coli protein-L-methionine + thioredoxin disulfide + H2O
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.4.11 37
-
 assay at Escherichia coli
1.8.4.12 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.11 7.4
-
 assay at Escherichia coli
1.8.4.12 7.4
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 dithiothreitol MsrA can also utilize DTT as reductant, the membrane-isozyme shows only poor activity, while MsrA1 is not active with DTT Escherichia coli
1.8.4.11 thioredoxin
-
 Escherichia coli
1.8.4.12 dithiothreitol MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity Escherichia coli
1.8.4.12 thioredoxin
-
 Escherichia coli