CYP7A1
CYP7A1 (cytochrome P450 family 7 subfamily A member 1, also known as CYP7) is an endoplasmic reticulum monooxygenase that catalyses the first reaction in the cholesterol catabolic pathway in the liver. It is a critical regulatory enzyme of bile acid biosynthesis and cholesterol homeostasis. Browse Assay Genie's current range of CYP7A1 research reagents below, or read on for the biology behind the target.
CYP7A1 is a cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives, the oxysterols. 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 (CPR). Its best-known reaction is hydroxylation of the carbon-hydrogen bond at the 7-alpha position of cholesterol. This is the rate-limiting step in cholesterol catabolism and bile acid biosynthesis, and it makes the enzyme the major site of regulation of bile acid synthesis, the primary mechanism for removing cholesterol from the body.
Beyond cholesterol, CYP7A1 7-alpha hydroxylates several oxysterols, including 4beta-hydroxycholesterol and 24-hydroxycholesterol. It also catalyses oxidation of the 7,8 double bond of 7-dehydrocholesterol and lathosterol, forming the 7-keto derivatives directly and predominantly. The protein is an endoplasmic reticulum membrane protein, found in the microsome membrane fraction, and acts in the liver. The human CYP7A1 gene encodes a member of the cytochrome P450 superfamily, whose monooxygenases catalyse many reactions in drug metabolism and in the synthesis of cholesterol, steroids and other lipids. Mouse and rat both have a Cyp7a1 ortholog.
The HGNC gene group is cytochrome P450 family 7. Earlier names include cytochrome P450, subfamily VIIA (cholesterol 7 alpha-monooxygenase), polypeptide 1, and the symbol CYP7 is still seen in the literature. Polymorphisms in the promoter of the CYP7A1 gene are associated with defects in bile acid synthesis, which makes it a reference point for studies of bile acid regulation and cholesterol balance.
CYP7A1 catalyses the rate-limiting step of bile acid synthesis and is the major site of its regulation.
As the first enzyme in hepatic cholesterol catabolism, it underpins the main route by which cholesterol is removed from the body.
CYP7A1 7-alpha hydroxylates oxysterols such as 4beta-hydroxycholesterol and 24-hydroxycholesterol, linking it to oxysterol turnover.
Its NADPH and cytochrome P450 reductase-dependent oxygen insertion makes it a useful model for P450 monooxygenase mechanism.
CYP7A1 hydroxylates cholesterol at the 7-alpha position, the first and rate-limiting reaction in converting cholesterol to bile acids in the liver. This makes it a critical regulatory enzyme of bile acid biosynthesis and cholesterol homeostasis. It also acts on several oxysterols and on 7-dehydrocholesterol and lathosterol.
Yes. The symbol CYP7 is an alias, and earlier HGNC names include cytochrome P450, subfamily VIIA (cholesterol 7 alpha-monooxygenase), polypeptide 1. The current approved name is cytochrome P450 family 7 subfamily A member 1. UniProt lists the protein as cytochrome P450 7A1.
Mouse and rat each have a Cyp7a1 ortholog. In humans, polymorphisms in the CYP7A1 promoter are associated with defects in bile acid synthesis. Check the datasheet of any product for its validated reactivity.
Other cytochrome P450 enzymes involved in sterol, steroid and xenobiotic metabolism with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P22680; product specifications from Assay Genie datasheets.