Sumpor oksigenaza/reduktaza
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| Sumpor oksigenaza/reduktaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Homo24mer SOR (Acidianus ambivalens) | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.13.11.55 | ||||||||
| CAS broj | 120598-92-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Sumpor oksigenaza/reduktaza (EC 1.13.11.55, SOR, sumporna oksigenaza, sumporna oksigenaza reduktaza) je enzim sa sistematskim imenom sumpor:kiseonik oksidoreduktaza (formira vodonik-sulfid- and sulfit).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 4 sumpor + 4H2O + O2 2 vodonik sulfid + 2 bisulfit + 2 H+
Ovaj enzim je prisutan u termofilnim mikroorganizmima. On sadrži u svakoj podjedinici jedan atom gvožđa koje nije vezano za hem. Elementrni sumpor je elektronski donor i jedan od akceptora. Kiseonik takođe može da bude akceptor.
Reference[uredi | uredi kod]
- ↑ Kletzin, A. (1989). „Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens”. J. Bacteriol. 171: 1638-1643. PMID 2493451.
- ↑ Kletzin, A. (1992). „Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens”. J. Bacteriol. 174: 5854-5859. PMID 1522063.
- ↑ Sun, C.W., Chen, Z.W., He, Z.G., Zhou, P.J. and Liu, S.J. (2003). „Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5”. Extremophiles 7: 131-134. PMID 12664265.
- ↑ Urich, T., Bandeiras, T.M., Leal, S.S., Rachel, R., Albrecht, T., Zimmermann, P., Scholz, C., Teixeira, M., Gomes, C.M. and Kletzin, A. (2004). „The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre”. Biochem. J. 381: 137-146. PMID 15030315.
Literatura[uredi | uredi kod]
- 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.