Glutation-disulfid reduktaza
| Glutation-disulfid reduktaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 PDB prikaz baziran na 1GRE. | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.8.1.7 | ||||||||
| CAS broj | 9001-48-3 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Glutation-disulfid reduktaza (EC 1.8.1.7, glutationska reduktaza, glutationska reduktaza (NADPH), NADPH-glutationska reduktaza, GSH reduktaza, GSSG reduktaza, NADPH-GSSG reduktaza, glutationska S-reduktaza, NADPH:oksidovani-glutation oksidoreduktaza) je enzim sa sistematskim imenom glutation:NADP+ oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2 glutation + NADP+ glutation disulfid + NADPH + H+
Ovaj enzim je dimerni flavoprotein (FAD). Njegova aktivnost je zavisna od redoks-aktivnog disulfida u svakom od aktivnih mesta.
Reference
- ^ Pai, E.F., Schirmer, R.H. and Schulz, G.E. (1978). „Structural studies on crystalline glutathione reductase from human erythrocytes”. Ур.: Singer, T.P. and Ondarza, R.N. Mechanisms of Oxidizing Enzymes. New York: Mechanisms of Oxidizing Enzymes. стр. 17—22. CS1 одржавање: Вишеструка имена: списак аутора (веза)
- ^ Pigiet, V.P. & Conley, R.R. (1977). „Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography”. J. Biol. Chem. 252: 6367—6372. PMID 330529.
- ^ Racker, E. (1955). „Glutathione reductase from bakers' yeast and beef liver”. J. Biol. Chem. 217: 855—865. PMID 13271446.
- ^ van Heyningen, R. & Pirie, A. (1953). „Reduction of glutathione coupled with oxidative decarboxylation of malate in cattle lens”. Biochem. J. 53: 436—444. PMID 13032091.
- ^ Worthington, D.J. & Rosemeyer, M.A. (1976). „Glutathione reductase from human erythrocytes. Catalytic properties and aggregation”. Eur. J. Biochem. 67: 231—238. PMID 9277.
- ^ Böhmé, C.C., Arscott, L.D., Becker, K., Schirmer, R.H. and Williams, C.H., Jr. (2000). „Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme”. J. Biol. Chem. 275: 37317—37323. PMID 10969088. CS1 одржавање: Вишеструка имена: списак аутора (веза)
- ^ Libreros-Minotta, C.A., Pardo, J.P., Mendoza-Hernandez, G. and Rendon, J.L. (1992). „Purification and characterization of glutathione reductase from Rhodospirillum rubrum”. Arch. Biochem. Biophys. 298: 247—253. PMID 1524433. CS1 одржавање: Вишеструка имена: списак аутора (веза)
Literatura
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
- Glutathione-disulfide+reductase на US National Library of Medicine Medical Subject Headings (MeSH)
- п
- р
- у
Oksidoreduktaze: Sumporne oksidoreduktaze (EC 1.8)
- Dihidrolipoil dehidrogenaza
- Glutation-disulfid reduktaza
- Tioredoksin-disulfid reduktaza
- Glutation dehidrogenaza (askorbat)
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