Peptid-metionin (R)-S-oksid reduktaza
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-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-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 uredi
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Ezraty, B., Aussel, L. and Barras, F. (2005). „Methionine sulfoxide reductases in prokaryotes”. Biochim. Biophys. Acta 1703: 221-229. PMID 15680230.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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 uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.