CYP4F2
| Cytochrome P450 4F2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Protein structure of cytochrome P450 4F2 (leukotriene-B4 omega-hydroxylase 1) enzyme | |||||||||
| Identifiers | |||||||||
| EC no. | 1.14.14.94 | ||||||||
| CAS no. | 90119-11-2 | ||||||||
| Alt. names | CYP4F2, 20-HETE synthase; 20-hydroxyeicosatetraenoic acid synthase; CYPIVF2; arachidonic acid omega-hydroxylase; cytochrome P450, family 4, subfamily F, polypeptide 2; cytochrome P450, subfamily IVF, polypeptide 2; cytochrome P450-LTB-omega; docosahexaenoic acid omega-hydroxylase; leucotriene-B4 ω-hydroxylase; leukotriene-B(4) 20-monooxygenase 1; leukotriene-B(4) omega-hydroxylase 1; LTB4 omega-hydroxylase; phylloquinone omega-hydroxylase CYP4F2. | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Cytochrome P450 4F2 (CYP4F2) is a human enzyme belonging to the cytochrome P450 (CYP) superfamily. It plays a key role in regulating inflammation by inactivating leukotriene B4, a potent inflammatory mediator, and is clinically significant because genetic variations in its encoding gene (CYP4F2, part of a cluster of cytochrome P450 genes on chromosome 19) affect the dosing of the anticoagulant warfarin.
CYP enzymes function primarily as monooxygenases, adding a hydroxy group to their substrates. They are most highly expressed in the liver and are responsible for about 80% of oxidative metabolism and about 50% of the elimination of commonly used drugs in humans.
The primary substrate of CYP4F2 is leukotriene B4 (LTB4), an eicosanoid inflammatory mediator. By hydroxylating LTB4 to its inactivated form 20-hydroxy-LTB4, the enzyme helps regulate inflammation. CYP4F2 also metabolizes other eicosanoids derived from arachidonic acid in white blood cells.
CYP4F2 also metabolizes certain fatty acids and fat-soluble vitamins, including vitamin E and vitamin K, and bioactivates prodrugs such as pafuramidine. Genetic variations in CYP4F2 affect enzymatic activity, with implications for vitamin K bioavailability and the dosing of vitamin K antagonists like warfarin.