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 4D6Z
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure-Based Inhibitor Design for Evaluation of a Cyp3A4 Pharmacophore Model.
Kaur, P., Chamberlin, R., Poulos, T.L., Sevrioukova, I.F.
J.Med.Chem.
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