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CYP2A7
CYP2A7 (cytochrome P450 family 2 subfamily A member 7, also known as CYP2A) is a xenobiotic-metabolizing monooxygenase of the endoplasmic reticulum. It can hydroxylate species-specific aromatic amine substrates and diclofenac in vitro, pointing to a potential role in drug metabolism. Browse Assay Genie's current range of CYP2A7 research reagents below, or read on for the biology behind the target.
CYP2A7 is a xenobiotic-metabolizing enzyme that can catalyse the hydroxylation of species-specific aromatic amine substrates. In vitro, it converts diclofenac to a hydroxydiclofenac metabolite, which suggests a potential role in drug metabolism. It does not metabolise nicotine, coumarin or 7-ethoxycoumarin, a profile that distinguishes it from some other members of the CYP2A subfamily. The enzyme is assigned EC 1.14.14.1 and is found in the endoplasmic reticulum and microsome membranes.
The CYP2A7 gene encodes a member of the cytochrome P450 superfamily. Cytochrome P450 proteins are monooxygenases that catalyse many reactions involved in drug metabolism and in the synthesis of cholesterol, steroids and other lipids. According to the NCBI Gene summary, the physiological substrate of the CYP2A7 protein has not yet been determined, so researchers should treat its biological role as incompletely defined. The gene produces two transcript variants.
The CYP2A7 gene sits within a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. HGNC places it in the cytochrome P450 family 2 gene group. Earlier nomenclature described it as cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 7, and CYP2A is listed as an alias. Comparison with neighbouring genes such as CYP2A6 and CYP2A13 is a common starting point for studying this locus.
CYP2A7 hydroxylates diclofenac in vitro, so it is relevant to studies of xenobiotic handling and the contribution of P450 enzymes to drug metabolism.
As a xenobiotic-metabolizing enzyme acting on aromatic amine substrates, CYP2A7 is of interest for work on how species-specific compounds are oxidised.
CYP2A7 does not metabolise nicotine, coumarin or 7-ethoxycoumarin, making it a useful point of contrast when comparing substrate specificity within the CYP2A cluster.
The substrate of CYP2A7 has not yet been determined, so it is a candidate for studies aiming to define the function of poorly characterised P450 enzymes.
CYP2A7 is a cytochrome P450 monooxygenase that can hydroxylate species-specific aromatic amine substrates. In vitro it converts diclofenac to hydroxydiclofenac, suggesting a role in drug metabolism. It does not metabolise nicotine, coumarin or 7-ethoxycoumarin. Its physiological substrate has not yet been determined.
The HGNC name is cytochrome P450 family 2 subfamily A member 7, and UniProt calls the protein cytochrome P450 2A7. CYP2A is listed as an alias. Older names include cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 7. The gene produces two transcript variants.
The CYP2A7 gene lies in a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. It belongs to the cytochrome P450 family 2 gene group. No mouse or rat ortholog is given in the data here, so check the datasheet of any product for its validated reactivity.
Other CYP2A subfamily members, cytochrome P450 family 2 enzymes and drug-metabolising P450s with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P20853; product specifications from Assay Genie datasheets.
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