CYP4F2

Cytochrome P450 4F2
Protein structure of cytochrome P450 4F2 (leukotriene-B4 omega-hydroxylase 1) enzyme[1]
Identifiers
EC no.1.14.14.94
CAS no.90119-11-2
Alt. namesCYP4F2, 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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
CYP4F2
Identifiers
AliasesCYP4F2, CPF2, cytochrome P450 family 4 subfamily F member 2
External IDsOMIM: 604426; MGI: 1919304; HomoloGene: 128623; GeneCards: CYP4F2; OMA:CYP4F2 - orthologs
EC number1.14.14.94
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001082

NM_024444

RefSeq (protein)

NP_001073

NP_077764

Location (UCSC)Chr 19: 15.88 – 15.9 MbChr 8: 72.74 – 72.76 Mb
PubMed search[4][5]
Wikidata
View/Edit HumanView/Edit Mouse

Cytochrome P450 4F2 is a protein that in humans is encoded by the CYP4F2 gene. This protein is an enzyme, a type of protein that catalyzes (helps speed up) chemical reactions inside cells. This specific enzyme is part of the superfamily of cytochrome P450 (CYP) enzymes, and the encoding gene is part of a cluster of cytochrome P450 genes located on chromosome 19.

CYP enzymes (CYPs) function primarily as monooxygenases (that add one hydroxy group (−OH) to a molecule). CYPs are membrane-bound and expressed in many cells, but are most highly expressed in the liver. CYPs contain heme (a precursor to hemoglobin) and hence are classified as hemoproteins. CYPs are involved in cellular metabolism, hormone synthesis, sterol and cholesterol metabolism, and are critical in maintaining homeostasis, a process by which an organism can maintain internal stability while adjusting to changing external conditions. In humans, CYPs are responsible for about 80% of oxidative metabolism and 50% of the removal of commonly used medical drugs. In addition, CYPs are often disease modifying and hence are frequent drug targets.

In the case of this specific enzyme, its primary substrate (molecule upon which an enzyme acts) is leukotriene B4 (LTB4), an eicosanoid, which is an inflammatory mediator. By hydroxylating LTB4 to its inactivated form 20-hydroxy-LTB4, this enzyme helps regulate inflammation levels in the body for a proper immune response. This enzyme also metabolizes other eicosanoids, a class of compounds produced in leukocytes (white blood cells) by the oxidation of arachidonic acid to regulate immune inflammation promoters.

The other substrates for this enzyme are certain fatty acids and vitamins. The enzyme bioactivates specific prodrugs into their active metabolites (for example, it converts the prodrug pafuramidine into its active form, furamidine). Variations in the gene can affect enzymatic activity, which has implications for drug dosing and bioavailability of fat-soluble vitamins such as vitamin E and vitamin K. In particular, variations affecting vitamin K bioavailability impact the dosing of vitamin K antagonists like warfarin or coumarin.

  1. ^ "Computed structure model of Cytochrome P450 4F2". RCSB Protein Data Bank. 30 September 2022. AF_AFP78329F1. Archived from the original on 26 November 2023. Retrieved 26 November 2023. Structure of heme (represented as spheres) copied from PDB: 6C94​ after alignment to AF_AFP78329F1.
  2. ^ a b c GRCh38: Ensembl release 89: ENSG00000186115Ensembl, May 2017
  3. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003484Ensembl, May 2017
  4. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.