Recombinant Human CYP2W1 Protein

Tag: N-MBP & C-His. Modification: unmodified. Start Site: Glu141. End Site: Leu280. Coverage: 0.3. Isoelectric Point: 5.5. Core Sequence: EPVADKILQE LKCLSGQLDG YRGRPFPLAL LGWAPSNITF ALLFGRRFDY RDPVFVSLLG LIDEVMVLLG SPGLQLFNVY PWLGALLQLH RPVLRKIEEV RAILRTLLEA RRPHVCPGDP VCSYVDALIQ QGQGDDPEGL. Homologies: Highest protein sequence identity to the following orthologs: Mouse - 73%, Rat - 39%, Pig - 83%, Cynomolgus monkey - 97%, Protein Function: 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:22591743, PubMed:26936974). May play a role in tumorigenesis by activating procarcinogens such as aflatoxin B1, polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines (PubMed:16551781, PubMed:20805301, 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) [The Uniprot Consortium]