Peptid-metionin (R)-S-oksid reduktaza

Peptid-metionin (R)-S-oksid reduktaza
Identifikatori
EC broj 1.8.4.12
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Peptid-metionin (R)-S-oksid reduktaza (EC 1.8.4.12, MsrB, metionin sulfoksidna reduktaza (nespecifična), pMSR, metionin S-oksidna reduktaza (nespecifična), selenoprotein R, metionin S-oksidna reduktaza (oksiduje R-formu), metionin sulfoksid reduktaza B, SelR, SelX, PilB, pRMsr) je enzim sa sistematskim imenom peptid-metionin:tioredoksin-disulfid S-oksidoreduktaza (formira metionin (R)-S-oksid).[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

peptid-L-metionin + tioredoksin disulfid +H2O peptid-L-metionin (R)-S-oksid + tioredoksin

Ova reakcija teče u reverznom smeru. Enzim manifestuje visoku specifičnost za redukciju R-forme L-metionin S-oksida. On brže deluje na L-metionin S-oksid nego na D-metionin S-oksid. Aktivnost je veća na ostataku peptida nego na slobodnoj aminokiselini.

Reference

  1. ↑ Moskovitz, J., Singh, V.K., Requena, J., Wilkinson, B.J., Jayaswal, R.K. and Stadtman, E.R. (2002). „Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity”. Biochem. Biophys. Res. Commun. 290: 62-65. PMID 11779133. 
  2. ↑ Taylor, A.B., Benglis, D.M., Jr., Dhandayuthapani, S. and Hart, P.J. (2003). „Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine”. J. Bacteriol. 185: 4119-4126. PMID 12837786. 
  3. ↑ Singh, V.K. and Moskovitz, J. (2003). „Multiple methionine sulfoxide reductase genes in Staphylococcus aureus: expression of activity and roles in tolerance of oxidative stress”. Microbiology 149: 2739-2747. PMID 14523107. 
  4. ↑ Boschi-Muller, S., Olry, A., Antoine, M. and Branlant, G. (2005). „The enzymology and biochemistry of methionine sulfoxide reductases”. Biochim. Biophys. Acta 1703: 231-238. PMID 15680231. 
  5. ↑ Ezraty, B., Aussel, L. and Barras, F. (2005). „Methionine sulfoxide reductases in prokaryotes”. Biochim. Biophys. Acta 1703: 221-229. PMID 15680230. 
  6. ↑ Weissbach, H., Resnick, L. and Brot, N. (2005). „Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage”. Biochim. Biophys. Acta 1703: 203-212. PMID 15680228. 
  7. ↑ Kauffmann, B., Aubry, A. and Favier, F. (2005). „The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions”. Biochim. Biophys. Acta 1703: 249-260. PMID 15680233. 
  8. ↑ Vougier, S., Mary, J. and Friguet, B. (2003). „Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells”. Biochem. J. 373: 531-537. PMID 12693988. 
  9. ↑ Olry, A., Boschi-Muller, S., Marraud, M., Sanglier-Cianferani, S., Van Dorsselear, A. and Branlant, G. (2002). „Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis”. J. Biol. Chem. 277: 12016-12022. PMID 11812798. 
  10. ↑ Sagher, D., Brunell, D., Hejtmancik, J.F., Kantorow, M., Brot, N. and Weissbach, H. (2006). „Thionein can serve as a reducing agent for the methionine sulfoxide reductases”. Proc. Natl. Acad. Sci. USA 103: 8656-8661. PMID 16735467. 

Literatura

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