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 2C9 |
Enzyme Information
| 1.14.14.51 |
(S)-limonene 6-monooxygenase.
based on mapping to UniProt P11712
(S)-limonene + [reduced NADPH--hemoprotein reductase] + O(2) = (-)-trans- carveol + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- The enzyme participates in the biosynthesis of (-)-carvone, which is responsible for the aroma of spearmint. -!- Formerly EC 1.14.13.48.
|
| 1.14.14.52 |
(S)-limonene 7-monooxygenase.
based on mapping to UniProt P11712
(S)-limonene + [reduced NADPH--hemoprotein reductase] + O(2) = (-)- perillyl alcohol + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- The enzyme, characterized from the plant Perilla frutescens, participates in the biosynthesis of perillyl aldehyde, the major constituent of the essential oil that accumulates in the glandular trichomes of this plant. -!- Some forms of the enzyme also catalyze the oxidation of (-)-perillyl alcohol to (-)-perillyl aldehyde. -!- Formerly EC 1.14.13.49.
|
| 1.14.14.- |
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.
based on mapping to UniProt P11712
|
| 1.14.14.53 |
(R)-limonene 6-monooxygenase.
based on mapping to UniProt P11712
(+)-(R)-limonene + [reduced NADPH--hemoprotein reductase] + O(2) = (+)- trans-carveol + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- The reaction is stereospecific with over 95% yield of (+)-trans- carveol from (R)-limonene. -!- (S)-Limonene, the substrate for EC 1.14.14.51 is not a substrate. -!- Forms part of the carvone biosynthesis pathway in Carum carvi (caraway) seeds. -!- Formerly EC 1.14.13.80.
|
UniProtKB Entries (1)
| P11712 |
CP2C9_HUMAN
Homo sapiens
Cytochrome P450 2C9
|
PDB Structure
| PDB | 5XXI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Basis of Single-Nucleotide Polymorphisms in Cytochrome P450 2C9
Biochemistry
|