Cijanatna hidrataza
(Preusmjereno sa stranice Cijanat hidrataza)
| Cijanatna hidrataza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 4.2.1.104 | ||||||||
| CAS broj | 37289-24-0 | ||||||||
| 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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Cijanatna hidrataza (EC 4.2.1.104, cijanatna lijaza, cijanatna hidrolaza, cijanatna aminohidrolaza, cijanatna C-N-lijaza) je enzim sa sistematskim imenom karbamat hidrolijaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- cijanat + HCO3- + 2 H+ NH3 + 2 CO2 (sveukupna reakcija)
- (1a) cijanat + HCO3- + H+ karbamat + CO2
- (1b) karbamat + H+ NH3 + CO2 (spontana reakcija)
Ovaj enzim, koji je pristuan u bakterijama i biljkama, posreduje razlaganje cijanata.
Reference[uredi | uredi kod]
- ↑ Anderson, P.M. (1980). „Purification and properties of the inducible enzyme cyanase”. Biochemistry 19: 2882-2888. PMID 6994799.
- ↑ Johnson, W.V. and Anderson, P.M. (1987). „Bicarbonate is a recycling substrate for cyanase”. J. Biol. Chem. 262: 9021-9025. PMID 3110153.
- ↑ Taussig, A. (1960). „T'he synthesis of the induced enzyme, "cyanase", in E. coli”. Biochim. Biophys. Acta 44: 510-519. PMID 13775509.
- ↑ Taussig, A. (1965). „Some properties of the induced enzyme cyanase”. Can. J. Biochem. 43: 1063-1069. PMID 5322950.
- ↑ Anderson, P.M., Korte, J.J. and Holcomb, T.A. (1994). „Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate”. Biochemistry 33: 14121-14125. PMID 7947823.
- ↑ Kozliak, E.I., Fuchs, J.A., Guilloton, M.B. and Anderson, P.M. (1995). „Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth by cyanate”. J. Bacteriol. 177: 3213-3219. PMID 7768821.
- ↑ Walsh, M.A., Otwinowski, Z., Perrakis, A., Anderson, P.M. and Joachimiak, A. (2000). „Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site”. Structure 8: 505-514. PMID 10801492.
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.