CATH Classification

Domain Context

CATH Clusters

Superfamily Cytochrome P450
Functional Family Cytochrome P450 3A4

Enzyme Information

1.14.14.56
1,8-cineole 2-exo-monooxygenase.
based on mapping to UniProt P08684
1,8-cineole + [reduced NADPH--hemoprotein reductase] + O(2) = 2-exo- hydroxy-1,8-cineole + [oxidized NADPH--hemoprotein reductase] + 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 1.14.14.55, EC 1.14.14.57 and EC 1.14.14.73. -!- Formerly EC 1.14.13.157.
1.14.14.55
Quinine 3-monooxygenase.
based on mapping to UniProt P08684
Quinine + [reduced NADPH--hemoprotein reductase] + O(2) = 3-hydroxyquinine + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- Formerly EC 1.14.13.67.
1.14.14.-
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.
based on mapping to UniProt P08684
1.14.14.73
Albendazole monooxygenase (sufoxide-forming).
based on mapping to UniProt P08684
(1) Albendazole + [reduced NADPH--hemoprotein reductase] + O(2) = albendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O. (2) Fenbendazole + [reduced NADPH--hemoprotein reductase] + O(2) = fenbendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- This is one of the activities carried out by some microsomal cytochrome P450 monooxygenases. -!- A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32), but it is estimated that cytochrome P450s are responsible for 70% of the activity.

UniProtKB Entries (1)

P08684
CP3A4_HUMAN
Homo sapiens
Cytochrome P450 3A4

PDB Structure

PDB 1W0G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal Structures of Human Cytochrome P450 3A4 Bound to Metyrapone and Progesterone
Williams, P.A., Cosme, J., Vinkovic, D.M., Ward, A., Angove, H.C., Day, P.J., Vonrhein, C., Tickle, I.J., Jhoti, H.
Science