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.

[16] The analysis of the gene on a molecular level presents several difficulties: Proteins consist of amino acid residues and form a three-dimensional structure.

Additionally, molecular docking has been employed to create a complex model of how CYP4F2 interacts with its substrates, to predict how the enzyme functions even without knowing its exact structure.

To test the functional hypotheses of CYP4 enzymes in non-mammalian vertebrates, researchers can use computational methods that compare the sequences, structures, and interactions of CYP4 proteins from different species.

[20] For example, one study used a computational approach to predict that the Cyp4d2 in a fruit fly (drosophila melanogaster), which is an ortholog of the human CYP4F2, may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.

[23] The Cyp4d2 in the fruit fly is expressed in the malpighian tubules, which are the insect equivalent of the kidneys, and may play a role in detoxification and osmoregulation.

[14][13] The localization of CYP4F2 to the smooth ER is important for its function and regulation, as it allows the enzyme to access its substrates and cofactors, and to be modulated by various factors, such as drugs, hormones, and dietary components.

In the clinical sciences they play critical roles in the detoxification of drugs, that is the process of breakdown and removing toxic substances from the body.

[30][29][14] Due to their role in many biological processes such as vascular constriction, sex hormone biosynthesis, and inflammatory response, CYP enzymes can be affected by therapy with the aim of modifying the course of diseases, a concept known as disease-modifying treatment.

[20] The cytochrome P450 4F2 protein is an enzyme also known as "leukotriene-B4 ω-hydroxylase 1", because it starts the process of inactivating and degrading leukotriene B4 (LTB4), a potent mediator of inflammation, by ω-hydroxylating it to 20-hydroxy-LTB4.

[20] CYP4F11 and CYP4F12 also metabolize VLCFA and display a unique feature in the CYP4F subfamily, as they are able to hydroxylate xenobiotics such as certain amphetamines, opioids, and macrolide antibiotics.

[36][38] As for the CYP4F2, besides its role in degrading LTB4, this enzyme is also involved in the metabolism of various endogenous substrates such as fatty acids, eicosanoids, and numerous fat-soluble vitamins.

[52][50] It induces the activation of polymorphonuclear leukocytes, monocytes and fibroblasts, the production of superoxide and the release of cytokines to attract neutrophils.

LTB4 also stimulates the production of reactive oxygen species, cytokines, chemokines and cell adhesion molecules, which further amplify the inflammatory response.

[56][57] Excessive or prolonged inflammation can be harmful to the host, as it can cause tissue damage and chronic diseases, so that the inflammatory process must be tightly regulated and resolved in a timely manner.

[62][15] CYP4F2 belongs to cytochrome P450 omega hydroxylase set of enzymes that catalyze the addition of a hydroxy functional group (−OH) to a molecule of the fatty acid substrate.

These enzymatic reactions lead to the production of metabolites involved in regulating inflammatory and vascular responses in animals and humans.

[61][55] By reducing the activity of these fatty acid metabolites, ω-hydroxylation plays a role in dampening inflammatory pathways and maintaining immune system balance.

[55][65][15] These genetic variations may impact the function or expression level of the enzyme, influencing its ability to perform ω-hydroxylation reactions effectively.

The production of ω-hydroxylated metabolites from monoepoxides derived from linoleic acid leukotoxin and isoleukotoxin helps regulate inflammation by reducing their activity as pro-inflammatory mediators.

This enzymatic activity ensures efficient breakdown and clearance of these fatty acids, preventing accumulation that could lead to metabolic imbalances or contribute to disease pathology.

[46] Fatty acid chain shortening by CYP4F2 is performed by their α-, β-, and ω-oxidation, with the preferred pathway being the β-oxidation in the mitochondria and peroxisomes.

[90] Confirmed variations in in CYP4F2 serve as biomarkers for individual differences in response to warfarin—adjusting warfarin dosage based on genetic information has demonstrated a decrease in negative clinical outcomes.

[46] There can be interactions between the drugs that rely on CYP4F2 on their metabolism or bioactivation (e.g., fingolimod, furamidine, warfarin)[89][99] and the substances that inhibit or induce CYP4F2 expression, such as statins and peroxisomal proliferators (drugs to lower low-density lipoproteins and reduce risk of risk of cardiovascular disease), 25-hydroxycholesterol, vitamin K, ketoconazole (an antifungal medication), sesamin (a component of sesame oil), and others.

[14][36] In the tumor microenvironment, proinflammatory cytokines can induce or inhibit CYP4F2 and other enzymes, which can promote carcinogenesis and affect chemotherapy, leading to adverse effects, toxicity, or therapeutic failure.

[102] Targeting CYPs in preclinical and clinical trials for chemoprevention and chemotherapy has become an effective way to improve antitumor treatment outcomes.

[104] Still, they can also provide a mechanism for drug resistance due to their aberrant expression and their supporting roles in tumor progression and metastasis.

[35][14] In 1997, Heng et al. found that the human CYP4F2 gene is mapped to chromosome 19 based on analysis of monochromosomal human-rodent cell hybrids using PCR.

[106][14] In 2007, Stec et al. identified a SNP in the coding region of the CYP4F2 gene, resulting in a V433M substitution, denoted as CYP4F2*3, that was frequent in both African and European American samples (9 to 21% minor allele frequency).

[105][14] In 2010, Ross et al. genotyped 963 individuals from 7 geographic regions worldwide for the CYP4F2 V433M substitution, to understand better algorithms for warfarin dose adjustment.