Biology:Peptide-methionine (R)-S-oxide reductase
| Peptide-methionine (R)-S-oxide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.8.4.12 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) is an enzyme that catalyzes the chemical reaction
- peptide-L-methionine + thioredoxin disulfide + H2O [math]\displaystyle{ \rightleftharpoons }[/math] peptide-L-methionine (R)-S-oxide + thioredoxin
The 3 substrates of this enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, whereas its two products are peptide-L-methionine (R)-S-oxide and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]. Other names in common use include MsrB, methionine sulfoxide reductase (ambiguous), pMSR, methionine S-oxide reductase (ambiguous), selenoprotein R, methionine S-oxide reductase (R-form oxidizing), methionine sulfoxide reductase B, SelR, SelX, PilB, and pRMsr.
References
- Moskovitz J; Singh, VK; Requena, J; Wilkinson, BJ; Jayaswal, RK; Stadtman, ER (2002). "Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity". Biochem. Biophys. Res. Commun. 290 (1): 62–5. doi:10.1006/bbrc.2001.6171. PMID 11779133. https://zenodo.org/record/1229532.
- "Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine". J. Bacteriol. 185 (14): 4119–26. 2003. doi:10.1128/JB.185.14.4119-4126.2003. PMID 12837786.
- "Multiple methionine sulfoxide reductase genes in Staphylococcus aureus: expression of activity and roles in tolerance of oxidative stress". Microbiology 149 (Pt 10): 2739–47. 2003. doi:10.1099/mic.0.26442-0. PMID 14523107.
- "The enzymology and biochemistry of methionine sulfoxide reductases". Biochim. Biophys. Acta 1703 (2): 231–8. 2005. doi:10.1016/j.bbapap.2004.09.016. PMID 15680231.
- "Methionine sulfoxide reductases in prokaryotes". Biochim. Biophys. Acta 1703 (2): 221–9. 2005. doi:10.1016/j.bbapap.2004.08.017. PMID 15680230.
- "Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage". Biochim. Biophys. Acta 1703 (2): 203–12. 2005. doi:10.1016/j.bbapap.2004.10.004. PMID 15680228.
- "The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions". Biochim. Biophys. Acta 1703 (2): 249–60. 2005. doi:10.1016/j.bbapap.2004.09.008. PMID 15680233.
- "Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells". Biochem. J. 373 (Pt 2): 531–7. 2003. doi:10.1042/BJ20030443. PMID 12693988.
- "Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis". J. Biol. Chem. 277 (14): 12016–22. 2002. doi:10.1074/jbc.M112350200. PMID 11812798.
- "Thionein can serve as a reducing agent for the methionine sulfoxide reductases". Proc. Natl. Acad. Sci. U.S.A. 103 (23): 8656–61. 2006. doi:10.1073/pnas.0602826103. PMID 16735467.
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