Nespecifična monooksigenaza
Изглед
Nespecifična monooksigenaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.14.14.1 | ||||||||
CAS broj | 9038-14-6 | ||||||||
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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Nespecifična monooksigenaza (EC 1.14.14.1, microsomal monooksigenaza, ksenobiotik monooksigenaza, aril-4-monooksigenaza, aril hidrokarbon hidroksilaza, microsomal P-450, flavoprotein-vezani monooksigenaza, flavoprotein monooksigenaza) je enzim sa sistematskim imenom supstrat,redukovani-flavoprotein:kiseonik oksidoreduktaza (RH-hidroksilacija or -epoksidacija).[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17] Ovaj enzim katalizuje sledeću hemijsku reakciju
- RH + redukovani flavoprotein + O2 ROH + oksidovani flavoprotein + H2O
Nespecifična monooksigenaza je grupa hem-tiolatnih proteina (P-450), koji deluju na širok opseg supstrata uključujući mnoge ksenobiotike, steroide, masne kiseline, vitamine i prostaglandine.
Reference
[уреди | уреди извор]- ^ Booth, J. & Boyland, E. (1957). „The biochemistry of aromatic amines. 3. Enzymic hydroxylation by rat-liver microsomes”. Biochem. J. 66: 73—78. PMID 13426111.
- ^ Fujita, T. & Mannering, G.J. (1971). „Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene”. Chem. Biol. Interact. 3: 264—265. PMID 5132997.
- ^ Haugen, D.A. & Coon, M.J. (1976). „Properties of electrophoretically homogeneous phenobarbital-inducible and β-naphthoflavone-inducible forms of liver microsomal cytochrome P-450”. J. Biol. Chem. 251: 7929—7939. PMID 187601.
- ^ Imaoka, S., Inoue, K. and Funae, Y. (1988). „Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography”. Arch. Biochem. Biophys. 265: 159—170. PMID 3415241.
- ^ Johnson, E.F., Zounes, M. and Müller-Eberhard, U. (1979). „Characterization of three forms of rabbit microsomal cytochrome P-450 by peptide mapping utilizing limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis”. Arch. Biochem. Biophys. 192: 282—289. PMID 434823.
- ^ Kupfer, D., Miranda, G.K., Navarro, J., Piccolo, D.E. and Theoharides, A.D. (1979). „Effect of inducers and inhibitors of monooxygenase on the hydroxylation of prostaglandins in the guinea pig. Evidence for several monooxygenases catalyzing ω- and ω-1-hydroxylation”. J. Biol. Chem. 254: 10405—10414. PMID 489601.
- ^ Lang, M.A., Gielen, J.E. and Nebert, D.W. (1981). „Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice”. J. Biol. Chem. 256: 12068—12075. PMID 7298645.
- ^ Lang, M.A. & Nebert, D.W. (1981). „Structural gene products of the Ah locus. Evidence for many unique P-450-mediated monooxygenase activities reconstituted from 3-methylcholanthrene-treated C57BL/6N mouse liver microsomes”. J. Biol. Chem. 256: 12058—12075. PMID 7298644.
- ^ Leo, M.A., Lasker, J.M., Rauby, J.L., Kim, C.I., Black, M. and Lieber, C.S. (1989). „Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8”. Arch. Biochem. Biophys. 269: 305—312. PMID 2916844.
- ^ Lu, A.Y.H., Kuntzman, S.W., Jacobson, M. and Conney, A.H. (1972). „Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. II. Role of the cytochrome P-450 and P-448 fractions in drug and steroid hydroxylations”. J. Biol. Chem. 247: 1727—1734. PMID 4401153.
- ^ Mitoma, C., Posner, H.S., Reitz, H.C. and Udenfriend, S. (1956). „Enzymic hydroxylation of aromatic compounds”. Arch. Biochem. Biophys. 61: 431—441. PMID 13314626.
- ^ Mitoma, C. & Udenfriend, S. (1962). „Aryl-4-hydroxylase”. Methods Enzymol. 5: 816—819.
- ^ Napoli, J.L., Okita, R.T., Masters, B.S. and Horst, R.L. (1981). „Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite”. Biochemistry. 20: 5865—5871. PMID 7295706.
- ^ Nebert, D.W. & Gelboin, H.V. (1968). „Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme”. J. Biol. Chem. 243: 6242—6249. PMID 4387094.
- ^ Suhara, K., Ohashi, K., Takahashi, K. and Katagiri, M. (1988). „Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)beta”. Arch. Biochem. Biophys. 267: 31—37. PMID 3264134.
- ^ Theoharides, A.D. & Kupfer, D. (1981). „Evidence for different hepatic microsomal monooxygenases catalyzing ω- and (ω-1)-hydroxylations of prostaglandins E1 and E2. Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation”. J. Biol. Chem. 256: 2168—2175. PMID 7462235.
- ^ Thomas, P.E., Lu, A.Y.H., Ryan, D., West, S.B., Kawalek, J. and Levin, W. (1976). „Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448”. Mol. Pharmacol. 12: 746—758. PMID 825720.
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]- Unspecific+monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)