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Literature summary extracted from

  • Aachmann, F.L.; Sal, L.S.; Kim, H.Y.; Marino, S.M.; Gladyshev, V.N.; Dikiy, A.
    Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis (2010), J. Biol. Chem., 285, 33315-33323.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.12 U95C the mutant has a significantly decreased activity Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.4.12 L-methionine sulfone
-
 Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.12 Zn2+ MsrB1 is a zinc-containing protein 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
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.12 Mus musculus Q9JLC3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.12 dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
-
 Mus musculus dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin
-
 Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.12 methionine sulfoxide reductase B1
-
 Mus musculus
1.8.4.12 MSRB1
-
 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.12 thioredoxin
-
 Mus musculus