EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
EC 188.8.131.52 - Unspecific monooxygenase
IntEnz Enzyme Nomenclature
- RH + [reduced NADPH—hemoprotein reductase] + O2 = ROH + [oxidized NADPH—hemoprotein reductase] + H2O
A group of P-450 heme-thiolate proteins, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 184.108.40.206, NADPH—hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 220.127.116.11, alkane 1-monooxygenase, belong here.
Links to other databases
The biochemistry of aromatic amines. 3. Enzymic hydroxylation by rat-liver microsomes.Biochem. J. 66: 73-78 (1957).
Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene.Chem.-Biol. Interact. 3: 264-265 (1971). [PMID: 5132997]
Properties of electrophoretically homogeneous phenobarbital-inducible and β-naphthoflavone-inducible forms of liver microsomal cytochrome P-450.J. Biol. Chem. 251: 7929-7939 (1976). [PMID: 187601]
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 (1988). [PMID: 3415241]
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 (1979). [PMID: 434823]
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 (1979). [PMID: 489601]
Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice.J. Biol. Chem. 256: 12068-12075 (1981). [PMID: 7298645]
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 (1981). [PMID: 7298645]
Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8.Arch. Biochem. Biophys. 269: 305-312 (1989). [PMID: 2916844]
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 (1972). [PMID: 4401153]
Enzymic hydroxylation of aromatic compounds.Arch. Biochem. Biophys. 61: 431-441 (1956).
Aryl-4-hydroxylase.Methods Enzymol. 5: 816-819 (1962).
Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite.Biochemistry 20: 5865-5871 (1981). [PMID: 7295706]
Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme.J. Biol. Chem. 243: 6242-6249 (1968). [PMID: 4387094]
Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)βArch. Biochem. Biophys. 267: 31-37 (1988). [PMID: 3264134]
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 (1981). [PMID: 7462235]
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 (1976). [PMID: 825720]
[EC 18.104.22.168 created 1961 as EC 22.214.171.124, transferred 1965 to EC 126.96.36.199, transferred 1972 to EC 188.8.131.52 (EC 184.108.40.206 created 1972, incorporated 1976, EC 220.127.116.11 created 1972, incorporated 1984), modified 2015]