Ugljen-monoksid dehidrogenaza (citohrom b-561)
(Preusmjereno sa stranice CO dehydrogenase)
| Ugljen-monoksid dehidrogenaza (citohrom b-561) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.2.2.4 | ||||||||
| CAS broj | 395639-79-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Ugljen-monoksid dehidrogenaza (citohrom b-561) (EC 1.2.2.4, karbon monoksidna oksidaza, karbon monoksidna oksigenaza (citohrom b-561), karbon monoksid:metilnsko plavo oksidoreduktaza, CO dehidrogenaza, karbon-monoksidna dehidrogenaza) je enzim sa sistematskim imenom karbon monoksid, voda:citohrom b-561 oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- CO + H2O + 2 fericitohrom b-561 CO2 + 2 H+ + 2 ferocitohrom b-561
Ovaj enzim sadrži molibdopterin citozin dinukleotid, FAD i [2Fe-2S]-klustere. Kiseonik, metilensko plavo I jodonitrotetrazolijum hlorid mogu da deluju kao nefiziološki elektronski akceptori.
Reference[uredi | uredi kod]
- ↑ Meyer, O., Jacobitz, S. and Krüger, B. (1986). „Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria”. FEMS Microbiol. Rev. 39: 161-179.
- ↑ Jacobitz, S. and Meyer, O. (1989). „Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes and restoration of respiratory activities”. J. Bacteriol. 171: 6294-6299. PMID 2808305.
- ↑ Meyer, O. and Schlegel, H.-G. (1980). „Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans”. J. Bacteriol. 141: 74-80. PMID 7354006.
- ↑ Dobbek, H., Gremer, L., Meyer, O. and Huber, R. (1999). „Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine”. Proc. Natl. Acad. Sci. USA 96: 8884-8889. PMID 10430865.
- ↑ Hänzelmann, P., Dobbek, H., Gremer, L., Huber, R. and Meyer, O. (2000). „The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase”. J. Mol. Biol. 301: 1221-1235. PMID 10966817.
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.