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Literature summary for 1.8.4.11 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)

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

Protein Variants

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
MsrA
-
Bos taurus
peptide methionine sulfoxide reductase
-
Bos taurus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
dithiothreitol
-
Bos taurus
thioredoxin
-
Bos taurus