MsrB – L-methionine-R-sulfoxide reductase

WID MsrB View in model
Name L-methionine-R-sulfoxide reductase View in model
Cross references EC:, BiGG: METSOXR2, KEGG: R04120
Type chemical View in model
Stoichiometry [c]: H2O + MET + MG_124_MONOMER_oxMETSOXRL + MG_124_MONOMER View in model
Enzyme MG_448_MONOMER [c] View in model
Is spontaneous (pH 7.5, 25C, I = 0) False View in model
Forward kinetics Vmax = 66.0 1/min View in model
Process Process_Metabolism View in model
Comments reactive oxygen species (eg. Superoxide, hydroxyl radical, hydrogen peroxide, singlet oxygen) can oxidize methionine to methionine sulfoxide; possibly > 30% of methionine residues are oxidized [PUB_0133]. catalyzes thioredoxin-dependent reduction of free and protein-bound Met(O) to methionine [PUB_0129]; S enantiomer selectivity [PUB_0131]; required for virulence, influences in cytadherence [PUB_0132]. Boschi-Muller et al reported that thioredoxin and Zn2+ are required as cofactors [PUB_0131]. Kinetic parameters observed by Boschi-Muller et al: Vmax=1.1 1/s [PUB_0131].
  1. Boschi-Muller S, Olry A, Antoine M, Branlant G. The enzymology and biochemistry of methionine sulfoxide reductases. Biochim Biophys Acta 1703, 231-8 (2005). WholeCell: PUB_0131, PubMed: 15680231

  2. Brot N, Weissbach H. Peptide methionine sulfoxide reductase: biochemistry and physiological role. Biopolymers 55, 288-96 (2000). WholeCell: PUB_0133, PubMed: 11169920

  3. Dhandayuthapani S, Blaylock MW, Bebear CM, Rasmussen WG, Baseman JB. Peptide methionine sulfoxide reductase (MsrA) is a virulence determinant in Mycoplasma genitalium. J Bacteriol 183, 5645-50 (2001). WholeCell: PUB_0132, PubMed: 11544227

  4. Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci U S A 98, 12920-5 (2001). WholeCell: PUB_0129, PubMed: 11606777

Created 2012-10-01 15:08:52
Last updated 2012-10-01 15:17:24