CATH Classification

Domain Context

CATH Clusters

Superfamily Cytochrome P450
Functional Family Cytochrome P450 family monooxygenase

Enzyme Information

1.14.13.157
1,8-cineole 2-exo-monooxygenase.
based on mapping to UniProt P08684
1,8-cineole + NADPH + O(2) = 2-exo-hydroxy-1,8-cineole + NADP(+) + H(2)O.
-!- The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including stereoids, fatty acids, and xenobiotics. -!- Cf. EC 1.14.13.97, EC 1.14.13.67 and EC 1.14.13.32.
1.14.13.32
Albendazole monooxygenase.
based on mapping to UniProt P08684
Albendazole + NADPH + O(2) = albendazole S-oxide + NADP(+) + H(2)O.
1.14.13.97
Taurochenodeoxycholate 6-alpha-hydroxylase.
based on mapping to UniProt P08684
(1) Taurochenodeoxycholate + NADPH + O(2) = taurohyocholate + NADP(+) + H(2)O. (2) Lithocholate + NADPH + O(2) = hyodeoxycholate + NADP(+) + H(2)O.
-!- Requires cytochrome b5 for maximal activity. -!- Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. -!- In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid.
1.14.14.1
Unspecific monooxygenase.
based on mapping to UniProt P08684
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed 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, it forms a system in which two reducing equivalents are supplied by NADPH. -!- Some of the reactions attributed to EC 1.14.15.3 belong here. -!- Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1.
1.14.13.67
Quinine 3-monooxygenase.
based on mapping to UniProt P08684
Quinine + NADPH + O(2) = 3-hydroxyquinine + NADP(+) + H(2)O.
1.14.13.-
With NADH or NADPH as one donor, and incorporation of one atom of oxygen.
based on mapping to UniProt P08684

UniProtKB Entries (1)

P08684
CP3A4_HUMAN
Homo sapiens
Cytochrome P450 3A4

PDB Structure

PDB 1TQN
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The Structure of Human Microsomal Cytochrome P450 3A4 Determined by X-ray Crystallography to 2.05-A Resolution
Yano, J.K., Wester, M.R., Schoch, G.A., Griffin, K.J., Stout, C.D., Johnson, E.F.
J.Biol.Chem.