CYP1B1
CYP1B1 (cytochrome P450 family 1 subfamily B member 1, also known as CP1B and GLC3A) is a membrane-bound cytochrome P450 monooxygenase of the endoplasmic reticulum. It metabolises steroid hormones, retinoids, fatty acids and xenobiotics, and mutations in its gene are linked to primary congenital glaucoma. Browse Assay Genie's current range of CYP1B1 research reagents below, or read on for the biology behind the target.
CYP1B1 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 (NADPH--hemoprotein reductase). It forms 2- and 4-hydroxy derivatives of estrone and 17beta-estradiol, with predominant 4-hydroxylase activity toward estradiol, and converts testosterone and progesterone to B or D ring hydroxylated metabolites.
The enzyme may be a major source of all-trans retinoic acid in extrahepatic tissues, catalysing two successive oxidations of all-trans retinol to all-trans retinal and then to retinoic acid. It also epoxidises double bonds of certain polyunsaturated fatty acids, converting arachidonic acid into the 8,9-, 11,12- and 14,15-epoxyeicosatrienoic acid regioisomers, which act as lipid mediators in the vascular system. A separate dehydratase activity toward hydroperoxyeicosatetraenoates (HpETEs) is independent of cytochrome P450 reductase, NADPH and O2. In xenobiotic metabolism, CYP1B1 converts polycyclic aromatic hydrocarbons and heterocyclic aryl amine procarcinogens into DNA-damaging products.
The CYP1B1 gene encodes a member of the cytochrome P450 superfamily, and the protein is found at the endoplasmic reticulum and microsome membrane, with a mitochondrial location also reported. It plays a role in retinal vascular development, promoting retinal angiogenesis and capillary morphogenesis under hyperoxic conditions, and contributes to oxidative homeostasis and organisation of trabecular meshwork tissue through modulation of POSTN expression. Mutations in the gene are associated with primary congenital glaucoma, which explains the alias GLC3A and the earlier name referring to glaucoma 3, primary infantile. This suggests the enzyme metabolises a signalling molecule, possibly a steroid, involved in eye development.
CYP1B1 hydroxylates estrone and 17beta-estradiol, notably at the C-4 position, making it a focus for studies of hormone metabolism.
The enzyme oxidises all-trans retinol to retinal and then retinoic acid, and may be a major source of retinoic acid in extrahepatic tissues.
CYP1B1 converts polycyclic aromatic hydrocarbons and heterocyclic aryl amines into DNA-damaging products, relevant to procarcinogen activation research.
Mutations are associated with primary congenital glaucoma, and the enzyme supports retinal vascular development and trabecular meshwork function.
CYP1B1 is a cytochrome P450 monooxygenase that metabolises fatty acids, steroid hormones, retinoids and xenobiotics. It hydroxylates estradiol, produces all-trans retinoic acid from retinol, epoxidises arachidonic acid and activates procarcinogens such as polycyclic aromatic hydrocarbons.
CYP1B1 is also known as CP1B and GLC3A, and the protein is named cytochrome P450 1B1. Earlier gene names include cytochrome P450, subfamily I (dioxin-inducible), polypeptide 1 (glaucoma 3, primary infantile). The enzyme is classified as EC 1.14.14.1.
Orthologues exist in both mouse and rat, each named Cyp1b1. In humans, mutations in the CYP1B1 gene are associated with primary congenital glaucoma. Check the datasheet of any product for its validated reactivity.
Other cytochrome P450 enzymes involved in steroid, retinoid, vitamin and xenobiotic metabolism.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q16678; product specifications from Assay Genie datasheets.