CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.630 | Cytochrome p450 | |
1.10.630.10 | Cytochrome P450 |
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.
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UniProtKB Entries (1)
P08684 |
CP3A4_HUMAN
Homo sapiens
Cytochrome P450 3A4
|
PDB Structure
PDB | 5TE8 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural basis for regiospecific midazolam oxidation by human cytochrome P450 3A4.
Proc. Natl. Acad. Sci. U.S.A.
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