Mouse Anti-CYP2W1 Recombinant Antibody (XB0319) (V2LY-0125-LY981)

Cytochrome P450 Family 2 Subfamily W Member 1

A cytochrome P450 monooxygenase that may play a role in retinoid and phospholipid metabolism (PubMed:22591743, PubMed:26936974).

Catalyzes the hydroxylation of saturated carbon hydrogen bonds. Hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may regulate atRA clearance. Other retinoids such as all-trans retinol and all-trans retinal are potential endogenous substrates (PubMed:26936974).

Catalyzes both epoxidation of double bonds and hydroxylation of carbon hydrogen bonds of the fatty acyl chain of 1-acylphospholipids/2-lysophospholipids. Can metabolize various lysophospholipids classes including lysophosphatidylcholines (LPCs), lysophosphatidylinositols (LPIs), lysophosphatidylserines (LPSs), lysophosphatidylglycerols (LPGs), lysophosphatidylethanolamines (LPEs) and lysophosphatidic acids (LPAs) (PubMed:22591743).

Has low or no activity toward 2-acylphospholipids/1-lysophospholipids, diacylphospholipids and free fatty acids (PubMed:26936974, PubMed:22591743).

May play a role in tumorigenesis by activating procarcinogens such as aflatoxin B1, polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines (PubMed:20805301, PubMed:16551781, PubMed:24278521).

Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:22591743, PubMed:26936974).

Aflatoxin metabolic process Source: UniProtKB
Exogenous drug catabolic process Source: GO_Central
Organic acid metabolic process Source: GO_Central
Phospholipid metabolic process Source: UniProtKB
Retinoic acid catabolic process Source: UniProtKB
Xenobiotic metabolic process Source: UniProtKB

Cell membrane; Endoplasmic reticulum lumen; Microsome membrane. About 8% are expressed on the cell surface.