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Literature summary extracted from

  • Bar-Noy, S.; Moskovitz, J.
    Mouse methionine sulfoxide reductase B: effect of selenocysteine incorporation on its activity and expression of the seleno-containing enzyme in bacterial and mammalian cells (2002), Biochem. Biophys. Res. Commun., 297, 956-961.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.12 overexpression of wild-type and mutants in Escherichia coli, expression as N- or C-terminally 6His-tagged protein lowers the recombinant expression level to 3% of total enzyme expressed, labeling of expressed wild-type with 75SeMet Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.12 additional information construction of a non-selenomethionine mutant of MsrB by site-directed mutagenesis, exchange of the selenomethionine by Cys, Ala, or Ser, the Cys-enzyme shows reduced activity, the Ser- and Ala-enzymes are inactive, substrate specificity, overview Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.4.12 13000
-
 x * 13000, native wild-type MsrB, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Mus musculus together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell L-methionine + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.12 Mus musculus
-
 selenomethionine-containing enzyme MsrB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.12 recombinant C-terminally His-tagged wild-type and mutant MsrB to homogeneity Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O selenomethionine is essential for MsrB activity Mus musculus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.4.12 liver
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 additional information substrate specificity Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.4.12 ? x * 13000, native wild-type MsrB, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
1.8.4.12 methionine sulfoxide reductase B
-
 Mus musculus
1.8.4.12 MsrB
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.4.12 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.12 7.4
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.12 thioredoxin
-
 Mus musculus