Metilsterol monooksigenaza
| Metilsterol monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.72 | ||||||||
| CAS broj | 37256-80-7 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Metilsterol monooksigenaza (EC 1.14.13.72, metilsterolna hidroksilaza, 4-metilsterolna oksidaza, 4,4-dimetil-5alfa-holest-7-en-3beta-ol,vodonik-donor:kiseonik oksidoreduktaza (hidroksilacija)) je enzim sa sistematskim imenom 4,4-dimetil-5alfa-holest-7-en-3beta-ol,NAD(P)H:kiseonik oksidoreduktaza (hidroksilacija).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 4,4-dimetil-5alfa-holest-7-en-3beta-ol + 3 NAD(P)H + 3 H+ + 3 O2 3beta-hidroksi-4beta-metil-5alfa-holest-7-en-4alfa-karboksilat + 3 NAD(P)+ + 4H2O (sveukupna reakcija)
- (1a) 4,4-dimetil-5alfa-holest-7-en-3beta-ol + NAD(P)H + H+ + O2 4beta-hidroksimetil-4alfa-metil-5alfa-holest-7-en-3beta-ol + NAD(P)+ +H2O
- (1b) 4beta-hidroksimetil-4alfa-metil-5alfa-holest-7-en-3beta-ol + NAD(P)H + H+ + O2 3beta-hidroksi-4beta-metil-5alfa-holest-7-en-4alfa-karbaldehid + NAD(P)+ + 2H2O
- (1c) 3beta-hidroksi-4beta-metil-5alfa-holest-7-en-4alfa-karbaldehid + NAD(P)H + H+ + O2 3beta-hidroksi-4beta-metil-5alfa-holest-7-en-4alfa-karboksilat + NAD(P)+ + H2O
Za rad ovog enzima je neophodan citohrom b5. On takođe deluje na 4alfa-metil-5alfa-holest-7-en-3beta-ol.
Reference[уреди | уреди извор]
- ^ Rahier, A., Smith, M. and Taton, M. (1997). „The role of cytochrome b5 in 4α-methyl-oxidation and C5(6) desaturation of plant sterol precursors”. Biochem. Biophys. Res. Commun. 236: 434—437. PMID 9240456.
- ^ Pascal, S., Taton, M. and Rahier, A. (1993). „Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation”. J. Biol. Chem. 268: 11639—11654. PMID 8505296.
- ^ Kawata, S., Trzaskos, J.M. and Gaylor, J.L. (1986). „Affinity chromatography of microsomal enzymes on immobilized detergent-solubilized cytochrome b5”. J. Biol. Chem. 261: 3790—3799. PMID 3949790.
- ^ Fukushima, H., Grinstead, G.F. and Gaylor, J.L. (1981). „Total enzymic synthesis of cholesterol from lanosterol. Cytochrome b5-dependence of 4-methyl sterol oxidase”. J. Biol. Chem. 256: 4822—4826. PMID 7228857.
- ^ Brady, D.R., Crowder, R.D. and Hayes, W.J. (1980). „Mixed function oxidases in sterol metabolism. Source of reducing equivalents”. J. Biol. Chem. 255: 10624—10629. PMID 7430141.
- ^ Gaylor, J.L. & Mason, H.S. (1968). „Investigation of the component reactions of oxidative sterol demethylation. Evidence against participation of cytochrome P-450”. J. Biol. Chem. 243: 4966—4972. PMID 4234469.
- ^ Miller, W.L., Kalafer, M.E., Gaylor, J.L. and Delwicke, C.V. (1967). „Investigation of the component reactions of oxidative sterol demethylation. Study of the aerobic and anaerobic processes”. Biochemistry. 6: 2673—2678. PMID 4383278.
Literatura[уреди | уреди извор]
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze[уреди | уреди извор]
- Methylsterol+monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)
