Biology:Unspecific monooxygenase

Short description: Class of enzymes

unspecific monooxygenase
Identifiers
EC number	1.14.14.1
CAS number	62213-32-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction

RH + reduced flavoprotein + O₂ [math]\displaystyle{ \rightleftharpoons }[/math] ROH + oxidized flavoprotein + H₂O

The 3 substrates of this enzyme are RH (reduced substrate), reduced flavoprotein, and O₂, whereas its 3 products are ROH (oxidized substrate), oxidized flavoprotein, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing). Other names in common use include microsomal monooxygenase, xenobiotic monooxygenase, aryl-4-monooxygenase, aryl hydrocarbon hydroxylase, microsomal P-450, flavoprotein-linked monooxygenase, and flavoprotein monooxygenase. This enzyme participates in 7 metabolic pathways: fatty acid metabolism, androgen and estrogen metabolism, gamma-hexachlorocyclohexane degradation, tryptophan metabolism, arachidonic acid metabolism, linoleic acid metabolism, and metabolism of xenobiotics by cytochrome p450. It employs one cofactor, heme.

Structural studies

As of late 2007, 53 structures have been solved for this class of enzymes, with PDB accession codes 1BU7, 1BVY, 1DT6, 1FAG, 1FAH, 1JME, 1JPZ, 1N6B, 1NR6, 1OG2, 1OG5, 1P0V, 1P0W, 1P0X, 1PO5, 1PQ2, 1R9O, 1SMI, 1SMJ, 1SUO, 1TQN, 1W0E, 1W0F, 1W0G, 1YQO, 1YQP, 1Z10, 1Z11, 1ZO4, 1ZO9, 1ZOA, 2BDM, 2BMH, 2F9Q, 2FDU, 2FDV, 2FDW, 2FDY, 2HI4, 2HPD, 2IJ2, 2IJ3, 2IJ4, 2J0D, 2J1M, 2J4S, 2NNB, 2P85, 2PG5, 2PG6, 2PG7, 2UWH, and 2V0M.

References

• "The biochemistry of aromatic amines. 3. Enzymic hydroxylation by rat-liver microsomes". Biochem. J. 66 (1): 73–8. 1957. doi:10.1042/bj0660073. PMID 13426111. 
• "Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene". Chem. Biol. Interact. 3 (4): 264–5. 1971. doi:10.1016/0009-2797(71)90053-6. PMID 5132997. 
• "Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450". J. Biol. Chem. 251 (24): 7929–39. 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 (1): 159–70. 1988. doi:10.1016/0003-9861(88)90381-5. 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 (1): 282–9. 1979. doi:10.1016/0003-9861(79)90093-6. PMID 434823. 
• "Effect of inducers and inhibitors of monooxygenase on the hydroxylation of prostaglandins in the guinea pig. Evidence for several monooxygenases catalyzing omega- and omega-1-hydroxylation". J. Biol. Chem. 254 (20): 10405–14. 1979. PMID 489601. 
• "Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice". J. Biol. Chem. 256 (23): 12068–75. 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 (23): 12058–67. 1981. PMID 7298644. 
• "Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8". Arch. Biochem. Biophys. 269 (1): 305–12. 1989. doi:10.1016/0003-9861(89)90112-4. 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 (6): 1727–34. 1972. PMID 4401153. 
• "Enzymatic hydroxylation of aromatic compounds". Arch. Biochem. Biophys. 61 (2): 431–41. 1956. doi:10.1016/0003-9861(56)90366-6. PMID 13314626. 
• "Aryl-4-hydroxylase". Methods Enzymol. 5: 816–819. 1962. doi:10.1016/s0076-6879(62)05318-5. 
• "Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite". Biochemistry 20 (20): 5865–71. 1981. doi:10.1021/bi00523a033. PMID 7295706. 
• "Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme". J. Biol. Chem. 243 (23): 6242–9. 1968. PMID 4387094. 
• "Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)beta". Arch. Biochem. Biophys. 267 (1): 31–7. 1988. doi:10.1016/0003-9861(88)90004-5. PMID 3264134. 
• "Evidence for different hepatic microsomal monooxygenases catalyzing omega- and (omega-1)-hydroxylations of prostaglandins E1 and E2 Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation". J. Biol. Chem. 256 (5): 2168–75. 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 (5): 746–58. 1976. PMID 825720.