Sterol 14-demetilaza
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| Sterol 14-demetilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.70 | ||||||||
| CAS broj | 60063-87-8 | ||||||||
| 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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Sterol 14-demetilaza (EC 1.14.13.70, obtusufoliolna 14-demetilaza, lanosterolna 14-demetilaza, lanosterolna 14alfa-demetilaza, sterolna 14alfa-demetilaza) je enzim sa sistematskim imenom sterol,NADPH:kiseonik oksidoreduktaza (14-metil odvajanje).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- obtusifoliol + 3 O2 + 3 NADPH + 3 H+ 4alfa-metil-5alfa-ergosta-8,14,24(28)-trien-3beta-ol + format + 3 NADP+ + 4H2O
Ovaj hem-tiolatni enzim (P-450) katalizuje sukcesivne hidroksilacije 14alfa-metil grupe i C-15, čemu sledi eliminacija formata i formiranje 14(15) dvostruke veze.
Reference[uredi | uredi kod]
- ↑ Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A. (1997). „Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals”. Plant J. 11: 191-201. PMID 9076987.
- ↑ Aoyama, Y. and Yoshida, Y. (1991). „Different substrate specificities of lanosterol 14α-demethylase (P450-14DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol”. Biochem. Biophys. Res. Commun. 178: 1064-1071. PMID 1872829.
- ↑ Aoyama, Y. and Yoshida, Y. (1992). „The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases”. Biochem. Biophys. Res. Commun. 183: 1266-1272. PMID 1567403.
- ↑ Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton, D.H.R. (1972). „The removal of the 32-carbon atom as formic acid in cholesterol biosynthesis”. J. Chem. Soc. Chem. Commun.: 383-385.
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.