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Literature summary extracted from

  • Lowther, W.T.; Brot, N.; Weissbach, H.; Honek, J.F.; Matthews, B.W.
    Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase (2000), Proc. Natl. Acad. Sci. USA, 97, 6463-6468.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.11 overexpression of N-terminally His-tagged wild-type and mutant MsrAs in Escherichia coli Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 C107S site-directed mutagenesis, the mutant shows 14% increased activity with DTT and 4% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C107S/C218S site-directed mutagenesis, the mutant shows 78% reduced activity with DTT and 94% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C107S/C218S/C227S site-directed mutagenesis, the mutant shows 61% reduced activity with DTT and 92% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C107S/C227S site-directed mutagenesis, the mutant shows 4% reduced activity with DTT and 86% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C218S site-directed mutagenesis, the mutant shows 65% reduced activity with DTT and 78% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C218S/C227S site-directed mutagenesis, the mutant shows 58% reduced activity with DTT and 96% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C227S site-directed mutagenesis, the mutant shows 11% reduced activity with DTT and 81% with thioredoxin compared to the wild-type enzyme Bos taurus
1.8.4.11 C72S site-directed mutagenesis, inactive mutant, no disulfide bond in the mutant enzyme Bos taurus
1.8.4.11 C72S/C107S/C227S site-directed mutagenesis, inactuve mutant Bos taurus
1.8.4.11 C72S/C218S site-directed mutagenesis, inactive mutant Bos taurus
1.8.4.11 additional information free sulfhydryl content and disulfide bond numbers in wild-type and mutant enzymes, overview Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.11 additional information the enzyme does not require meal ions for activity, free sulfhydryl content and disulfide bond numbers in wild-type and mutant enzymes, overview Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.11 recombinant N-terminally His-tagged wild-type and mutant MsrAs from Escherichia coli by nickel affinity chromatography and dialysis Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.11 peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin catalytic mechanism, Cys72 is essential for activity forming disulfide bonds with either Cys218 or Cys227 Bos taurus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 N-acetyl-L-methionine-(S)-S-oxide + DTT stereospecific reduction Bos taurus N-acetyl-L-methionine + DTT disulfide + H2O
-
 ?
1.8.4.11 N-acetyl-L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Bos taurus N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 MsrA
-
 Bos taurus
1.8.4.11 peptide methionine sulfoxide reductase
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.4.11 37
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.11 7.4
-
 assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 dithiothreitol
-
 Bos taurus
1.8.4.11 thioredoxin
-
 Bos taurus