CYP1A1
CYP1A1 (cytochrome P450 family 1 subfamily A member 1, also known as P450DX, P1-450, P450-C, CP11 and CYP1) is a cytochrome P450 monooxygenase that hydroxylates carbon-hydrogen bonds in endogenous lipids, steroids and vitamins. Its expression is induced by some polycyclic aromatic hydrocarbons. Browse Assay Genie's current range of CYP1A1 research reagents below, or read on for the biology behind the target.
CYP1A1 is a cytochrome P450 monooxygenase involved in the metabolism of endogenous substrates including fatty acids, steroid hormones and vitamins. Mechanistically, it uses molecular oxygen, inserting one oxygen atom into the substrate and reducing the second to water, with two electrons supplied by NADPH through cytochrome P450 reductase. It catalyses the hydroxylation of carbon-hydrogen bonds. Among steroids, it shows high activity in forming hydroxyestrogens from estrone and 17beta-estradiol, producing the 2-hydroxy derivatives as well as C15-alpha and C16-alpha D-ring hydroxylated products.
The enzyme also acts on lipids. It hydroxylates polyunsaturated fatty acids with differing regioselectivities and epoxidises certain double bonds. It converts arachidonic acid to the 8,9-, 11,12- and 14,15-epoxyeicosatrienoic acid regioisomers, which act as lipid mediators in the vascular system, and shows absolute stereoselectivity in producing the 17(R),18(S) enantiomer from eicosapentaenoic acid. It may contribute to all-trans retinoic acid biosynthesis in extrahepatic tissues by oxidising all-trans retinol to retinal and then to retinoic acid, and may take part in eicosanoid metabolism through an NADPH-independent, lipoxygenase-like conversion of hydroperoxides to oxo metabolites.
The CYP1A1 gene encodes a member of the cytochrome P450 superfamily, whose enzymes catalyse many reactions in drug metabolism and in the synthesis of cholesterol, steroids and other lipids. The protein localises to the endoplasmic reticulum, and UniProt also reports it at the mitochondrial inner membrane, microsomes and cytoplasm. Its expression is induced by some polycyclic aromatic hydrocarbons, including some found in cigarette smoke, and it can metabolise some of them to carcinogenic intermediates. The gene has been associated with lung cancer risk. The related gene CYP1A2 lies about 25 kb away on the same chromosome, and alternative splicing yields multiple transcript variants encoding distinct isoforms.
CYP1A1 expression is induced by some polycyclic aromatic hydrocarbons, and the enzyme can convert some of them into carcinogenic intermediates.
The CYP1A1 gene has been associated with lung cancer risk, linking PAH exposure, including from cigarette smoke, to enzyme activity.
CYP1A1 forms 2-hydroxy and D-ring hydroxylated oestrogens from estrone and 17beta-estradiol with high catalytic activity.
The enzyme generates epoxyeicosatrienoic acids from arachidonic acid and may support all-trans retinoic acid synthesis in extrahepatic tissues.
CYP1A1 is a cytochrome P450 monooxygenase that inserts one oxygen atom into a substrate, using electrons from NADPH via cytochrome P450 reductase. It hydroxylates and epoxidises fatty acids, steroid hormones and vitamins, and can metabolise some polycyclic aromatic hydrocarbons to carcinogenic intermediates.
CYP1A1 is also called P450DX, P1-450, P450-C, CP11 and CYP1. Earlier HGNC names were cytochrome P450, subfamily I (aromatic compound-inducible), polypeptide 1, and cytochrome P450, family 1, subfamily A, polypeptide 1. Alternative splicing gives multiple transcript variants encoding distinct isoforms.
Mouse and rat both have a Cyp1a1 ortholog. In humans, the CYP1A1 gene has been associated with lung cancer risk, and the enzyme can convert some PAHs to carcinogenic intermediates. Check the datasheet of any product for its validated reactivity.
Other cytochrome P450 enzymes, including CYP1 family members and enzymes of steroid, retinoid and vitamin metabolism.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P04798; product specifications from Assay Genie datasheets.