Cytochrome P450 3A7
Also known as: CYP3A7
Function
A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins during embryogenesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes 3beta-hydroxyandrost-5-en-17-one (dehydroepiandrosterone, DHEA), a precursor in the biosynthesis of androgen and estrogen steroid hormones. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1), particularly D-ring hydroxylated estrone at the C16-alpha position. Mainly hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in atRA clearance during fetal development. Also involved in the oxidative metabolism of xenobiotics including anticonvulsants.
Classification
- Family (Pfam)
- PF00067 p450
- InterPro
- Cyt_P450, Cyt_P450_CS, Cyt_P450_E_CYP3A, Cyt_P450_E_grp-II, Cyt_P450_sf, Cytochrome_P450_3A
- Functional cluster
- Serine/Threonine Protein Kinases
Experimental structures · PDB · 2
A predicted model is available from AlphaFold.
Gene Ontology · 19
- GO:0005789 endoplasmic reticulum membrane
- GO:0062183 all-trans retinoic acid 18-hydroxylase activity
- GO:0101020 estrogen 16-alpha-hydroxylase activity
- GO:0101021 estrogen 2-hydroxylase activity
- GO:0020037 heme binding
- GO:0005506 iron ion binding
- GO:0004497 monooxygenase activity
- GO:0019825 oxygen binding
- GO:0008401 retinoic acid 4-hydroxylase activity
- GO:0008395 steroid hydroxylase activity
- GO:0050649 testosterone 6-beta-hydroxylase activity
- GO:0008210 estrogen metabolic process
- GO:0002933 lipid hydroxylation
- GO:0070989 oxidative demethylation
- GO:0042573 retinoic acid metabolic process
- GO:0042572 retinol metabolic process
- GO:0006694 steroid biosynthetic process
- GO:0008202 steroid metabolic process
- GO:0006805 xenobiotic metabolic process
Drugs targeting this protein · 2
- RITONAVIR inhibitor
- COBICISTAT inhibitor
Related proteins · sequence + function similarity
- Cytochrome P450 3A8 0.99
- Cytochrome P450 3A21 0.99
- Cytochrome P450 3A13 0.99
- Cytochrome P450 3A5 0.99
- Cytochrome P450 3A4 0.99
- Cytochrome P450 3A12 0.99
- Cytochrome P450 3A24 0.98
- Cytochrome P450 3A2 0.98
- Cytochrome P450 3A1 0.98
- Cytochrome P450 3A9 0.98
- Cytochrome P450 3A29 0.98
- Cytochrome P450 3A28 0.98
Co-cited proteins · studied together in the literature
- Cytochrome P450 3A5 3 shared papers
- Cytochrome P450 3A4 4 shared papers
- Cytochrome P450 3A43 1 shared papers
- Cytochrome P450 2C8 2 shared papers
- Cytochrome P450 2C18 1 shared papers
- Cytochrome P450 1A1 2 shared papers
- Cytochrome P450 2B6 1 shared papers
- Cytochrome P450 1B1 1 shared papers
- Cytochrome P450 2C9 1 shared papers
- Cytochrome P450 1A2 1 shared papers
Literature · 12 cited papers
- Helices F-G are important for the substrate specificities of CYP3A7. Drug Metab. Dispos. · 2007
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. · 2004
- Human cytochrome P450 3A7 has a distinct high catalytic activity for the 16alpha-hydroxylation of estrone but not 17beta-estradiol. Cancer Res. · 2003
- Characterization of the oxidative metabolites of 17beta-estradiol and estrone formed by 15 selectively expressed human cytochrome p450 isoforms. Endocrinology · 2003
- Human chromosome 7: DNA sequence and biology. Science · 2003
- Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics · 2001
- The human cytochrome P450 3A locus. Gene evolution by capture of downstream exons. Gene · 2000
- Identification of human cytochrome P450s involved in the formation of all-trans-retinoic acid principal metabolites. Mol. Pharmacol. · 2000
- Differential catalytic properties in metabolism of endogenous and exogenous substrates among CYP3A enzymes expressed in COS-7 cells. Biochim. Biophys. Acta · 1998
- Isolation of a new human fetal liver cytochrome P450 cDNA clone: evidence for expression of a limited number of forms of cytochrome P450 in human fetal livers. Arch. Biochem. Biophys. · 1989
- Molecular cloning and sequence analysis of cDNA containing the entire coding region for human fetal liver cytochrome P-450. J. Biochem. · 1989
- Isolation and characterization of human fetal liver cytochrome P450HLp2: a third member of the P450III gene family. Arch. Biochem. Biophys. · 1989