Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy

substrate,NADPH---hemoprotein reductase:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)

RH + [reduced NADPH---hemoprotein reductase] + O2 = ROH + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R04122]

R04122 > R01842 R02354 R02355 R02356 R02503 R03088 R03089 R03090 R03408 R03629 R04121;
(other) R03697 R05259 R07000 R07001 R07021 R07022 R07042 R07043 R07044 R07045 R07046 R07048 R07050 R07051 R07052 R07054 R07055 R07056 R07079 R07080 R07081 R07085 R07087 R07098 R07099 R07939 R07943 R07945 R08265 R08267 R08270 R08286 R08287 R08293 R08294 R08312 R08343 R08344 R08345 R08390 R08391 R08392 R09404 R09405 R09406 R09407 R09408 R09416 R09418 R09421 R09423 R09424 R09425 R09442
Reaction

RH [CPD:C01371];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]

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 1.6.2.4, NADPH---hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.

EC 1.14.14.1 created 1961 as EC 1.99.1.1, transferred 1965 to EC 1.14.1.1, transferred 1972 to EC 1.14.14.1 (EC 1.14.14.2 created 1972, incorporated 1976, EC 1.14.99.8 created 1972, incorporated 1984), modified 2015

1  [PMID:13426111]

BOOTH J, BOYLAND E.

The biochemistry of aromatic amines.  III.  Enzymic hydroxylation by rat-liver microsomes.

Biochem J 66:73-8 (1957)
DOI:10.1042/bj0660073

2  [PMID:5132997]

Fujita T, Mannering GJ.

Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene.

Chem Biol Interact 3:264-5 (1971)
DOI:10.1016/0009-2797(71)90053-6

3  [PMID:187601]

Haugen DA, Coon MJ.

Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450.

J Biol Chem 251:7929-39 (1976)

4  [PMID:3415241]

Imaoka S, Inoue K, Funae Y.

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 265:159-70 (1988)
DOI:10.1016/0003-9861(88)90381-5

5  [PMID:434823]

Johnson EF, Zounes MC, Muller-Eberhard U.

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 192:282-9 (1979)
DOI:10.1016/0003-9861(79)90093-6

6  [PMID:489601]

Kupfer D, Miranda GK, Navarro J, Piccolo DE, Theoharides AD.

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 254:10405-14 (1979)

7  [PMID:7298645]

Lang MA, Gielen JE, Nebert DW.

Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice.

J Biol Chem 256:12068-75 (1981)

8  [PMID:7298644]

Lang MA, Nebert DW.

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 256:12058-67 (1981)

9  [PMID:2916844]

Leo MA, Lasker JM, Raucy JL, Kim CI, Black M, Lieber CS

Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8.

Arch Biochem Biophys 269:305-12 (1989)
DOI:10.1016/0003-9861(89)90112-4

10 [PMID:4401153]

Lu AY, Kuntzman R, West S, Jacobson M, Conney AH.

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 247:1727-34 (1972)

11 [PMID:13314626]

MITOMA C, POSNER HS, REITZ HC, UDENFRIEND S.

Enzymatic hydroxylation of aromatic compounds.

Arch Biochem Biophys 61:431-41 (1956)
DOI:10.1016/0003-9861(56)90366-6

12

Mitoma, C. and Udenfriend, S.

Aryl-4-hydroxylase.

Methods Enzymol 5:816-819 (1962)

13 [PMID:7295706]

Napoli JL, Okita RT, Masters BS, Horst RL.

Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite.

Biochemistry 20:5865-71 (1981)
DOI:10.1021/bi00523a033

14 [PMID:4387094]

Nebert DW, Gelboin HV.

Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme.

J Biol Chem 243:6242-9 (1968)

15 [PMID:3264134]

Suhara K, Ohashi K, Takahashi K, Katagiri M.

Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)beta.

Arch Biochem Biophys 267:31-7 (1988)
DOI:10.1016/0003-9861(88)90004-5

16 [PMID:7462235]

Theoharides AD, Kupfer D.

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 256:2168-75 (1981)

17 [PMID:825720]

Thomas PE, Lu AY, Ryan D, West SB, Kawalek J, Levin W.

Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448.

Mol Pharmacol 12:746-58 (1976)