Holestanetriol 26-monooksigenaza
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| Holestanetriol 26-monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.15 | ||||||||
| CAS broj | 52227-77-7 | ||||||||
| 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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Holestanetriol 26-monooksigenaza (EC 1.14.13.15, 5beta-holestan-3alfa,7alfa,12alfa-triol 26-hidroksilaza, 5beta-holestan-3alfa,7alfa,12alfa-triol hidroksilaza, holestantriolna 26-hidroksilaza, sterolna 27-hidroksilaza, sterolna 26-hidroksilaza, holesterolna 27-hidroksilaza, CYP27A, CYP27A1, citohrom P450 27A1) je enzim sa sistematskim imenom 5beta-holestan-3alfa,7alfa,12alfa-triol,NADPH:kiseonik oksidoreduktaza (26-hidroksilacija).[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5beta-holestan-3alfa,7alfa,12alfa-triol + 3 NADPH + 3 H+ + 3 O2 (25R)-3alfa,7alfa,12alfa-trihidroksi-5beta-holestan-26-oat + 3 NADP+ + 4H2O (sveukupna reakcija)
- (1a) 5beta-holestan-3alfa,7alfa,12alfa-triol + NADPH + H+ + O2 (25R)-5beta-holestan-3alfa,7alfa,12alfa,26-tetraol + NADP+ +H2O
- (1b) (25R)-5beta-holestan-3alfa,7alfa,12alfa,26-tetraol + NADPH + H+ + O2 (25R)-3alfa,7alfa,12alfa-trihidroksi-5beta-holestan-26-al + NADP+ + 2H2O
- (1c) (25R)-3alfa,7alfa,12alfa-trihidroksi-5beta-holestan-26-al + NADPH+ + H+ + O2 (25R)-3alfa,7alfa,12alfa-trihidroksi-5beta-holestan-26-oat + NADP+ +H2O
Za rad ovog enzima su neophodni feredoksin i feredoksinska reduktaza.
Reference[uredi | uredi kod]
- ↑ Masui, T., Herman, R. and Staple, E. (1966). „The oxidation of 5β-cholestane-3α,7α,12α,26-tetraol to 5β-cholestane-3α,7α,12α-triol-26-oic acid via 5β-cholestane-3α,7α,12α-triol-26-al by rat liver”. Biochim. Biophys. Acta 117: 266-268. PMID 5914340.
- ↑ Okuda, K. and Hoshita, N. (1968). „Oxidation of 5β-cholestane-3α,7α,12α-triol by rat-liver mitochondria”. Biochim. Biophys. Acta 164: 381-388. PMID 4388637.
- ↑ Wikvall, K. (1984). „Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids”. J. Biol. Chem. 259: 3800-3804. PMID 6423637.
- ↑ Andersson, S., Davis, D.L., Dahlbäck, H., Jörnvall, H. and Russell, D.W. (1989). „Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme”. J. Biol. Chem. 264: 8222-8229. PMID 2722778.
- ↑ Dahlback, H. and Holmberg, I. (1990). „Oxidation of 5β-cholestane-3α,7α,12α-triol into 3α,7α,12α-trihydroxy-5β-cholestanoic acid by cytochrome P-45026 from rabbit liver mitochondria”. Biochem. Biophys. Res. Commun. 167: 391-395. PMID 2322231.
- ↑ Holmberg-Betsholtz, I., Lund, E., Björkhem, I. and Wikvall, K. (1993). „Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of oxidation of 5β-cholestane-3α,7α,12α,27-tetrol into 3α,7α,12α-trihydroxy-5β-cholestanoic acid”. J. Biol. Chem. 268: 11079-11085. PMID 8496170.
- ↑ Pikuleva, I.A., Babiker, A., Waterman, M.R. and Bjorkhem, I. (1998). „Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways”. J. Biol. Chem. 273: 18153-18160. PMID 9660774.
- ↑ Furster, C., Bergman, T. and Wikvall, K. (1999). „Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria”. Biochem. Biophys. Res. Commun. 263: 663-666. PMID 10512735.
- ↑ Pikuleva, I.A., Puchkaev, A. and Björkhem, I. (2001). „Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A1”. Biochemistry 40: 7621-7629. PMID 11412116.
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.