CYP1A2
CYP1A2 (cytochrome P450 1A2, also known as P3-450 or CP12) is an endoplasmic reticulum monooxygenase of the cytochrome P450 family. It hydroxylates carbon-hydrogen bonds in endogenous lipids, steroids and vitamins, and metabolises xenobiotics such as caffeine. Browse Assay Genie's current range of CYP1A2 research reagents below, or read on for the biology behind the target.
CYP1A2 is a cytochrome P450 monooxygenase. 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. The result is hydroxylation of carbon-hydrogen bonds. Endogenous substrates include fatty acids, steroid hormones and vitamins. The enzyme forms 2-hydroxy estrone and 2-hydroxy 17beta-estradiol with high catalytic activity, and it metabolises cholesterol towards 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis.
The enzyme may also be a major route to all-trans retinoic acid in the liver, catalysing two successive oxidations of all-trans retinol, first to all-trans retinal and then to retinoic acid. With polyunsaturated fatty acids it mainly catalyses stereoselective epoxidation of the last double bond, with a strong preference for the (R,S) stereoisomer. It also performs bisallylic and omega-1 hydroxylation, and may take part in eicosanoid metabolism by converting hydroperoxides to oxo metabolites in an NADPH-independent, lipoxygenase-like reaction. In xenobiotic metabolism, CYP1A2 catalyses N-hydroxylation of heterocyclic amines, O-deethylation of phenacetin and N3-demethylation of caffeine. Aflatoxin B1 and acetaminophen are also substrates.
The CYP1A2 gene encodes a protein that localises to the endoplasmic reticulum membrane, and the microsome fraction in fractionation studies. Its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), including some found in cigarette smoke. The enzyme can convert some PAHs into carcinogenic intermediates, although its endogenous substrate is still described as unknown. The transcript carries four Alu sequences flanked by direct repeats in the 3' untranslated region. HGNC places the gene in the cytochrome P450 family 1 group, and previous names refer to an aromatic compound-inducible subfamily.
CYP1A2 metabolises caffeine, phenacetin, acetaminophen and aflatoxin B1, making it a central enzyme for studying how foreign compounds are processed.
The enzyme converts some PAHs to carcinogenic intermediates and N-hydroxylates heterocyclic amines, which makes it relevant to studies of carcinogen activation.
CYP1A2 forms 2-hydroxyestrogens from estrone and estradiol and converts cholesterol towards 25-hydroxycholesterol, a regulator of cholesterol homeostasis.
It may drive hepatic all-trans retinoic acid synthesis and epoxidises or hydroxylates polyunsaturated fatty acids, linking it to retinoid and eicosanoid pathways.
CYP1A2 is a cytochrome P450 monooxygenase that hydroxylates carbon-hydrogen bonds using oxygen and NADPH-derived electrons. It acts on fatty acids, steroid hormones, retinol and cholesterol, and on xenobiotics including caffeine, phenacetin, heterocyclic amines and aflatoxin B1.
Aliases include P3-450 and CP12, and UniProt names the protein cytochrome P450 1A2. Earlier HGNC names described it as cytochrome P450, subfamily I (aromatic compound-inducible), polypeptide 2. The enzyme is classified as EC 1.14.14.1.
Yes. Mouse and rat both have an ortholog named Cyp1a2, so the enzyme can be studied in rodent models. Researchers should check the datasheet of any product for its validated reactivity before choosing a species.
Other cytochrome P450 enzymes involved in xenobiotic, steroid and retinoid metabolism, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P05177; product specifications from Assay Genie datasheets.