Aliases for CYP1B1 Gene
- Cytochrome P450 Family 1 Subfamily B Member 1 2 3 5
- Cytochrome P450, Subfamily I (Dioxin-Inducible), Polypeptide 1 (Glaucoma 3, Primary Infantile) 2 3
- Cytochrome P450, Family 1, Subfamily B, Polypeptide 1 2 3
- Hydroperoxy Icosatetraenoate Dehydratase 3 4
- Cytochrome P450 1B1 3 4
- EC 126.96.36.199 4 51
- CYPIB1 3 4
- CP1B 2 3
- Flavoprotein-Linked Monooxygenase 3
External Ids for CYP1B1 Gene
Previous HGNC Symbols for CYP1B1 Gene
Previous GeneCards Identifiers for CYP1B1 Gene
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The enzyme encoded by this gene localizes to the endoplasmic reticulum and metabolizes procarcinogens such as polycyclic aromatic hydrocarbons and 17beta-estradiol. Mutations in this gene have been associated with primary congenital glaucoma; therefore it is thought that the enzyme also metabolizes a signaling molecule involved in eye development, possibly a steroid. [provided by RefSeq, Jul 2008]
GeneCards Summary for CYP1B1 Gene
CYP1B1 (Cytochrome P450 Family 1 Subfamily B Member 1) is a Protein Coding gene. Diseases associated with CYP1B1 include Glaucoma 3, Primary Congenital, A and Anterior Segment Dysgenesis 6. Among its related pathways are Cytochrome P450 - arranged by substrate type and Arachidonic acid metabolism. Gene Ontology (GO) annotations related to this gene include iron ion binding and oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen. An important paralog of this gene is CYP1A2.
UniProtKB/Swiss-Prot Summary for CYP1B1 Gene
A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). 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) (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activity toward E2 at the C-4 position (PubMed:11555828, PubMed:12865317). Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (PubMed:10426814). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376, PubMed:15258110). Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system (PubMed:20972997). Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (PubMed:21068195). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products (PubMed:10426814). Plays an important role in retinal vascular development. Under hyperoxic O2 conditions, promotes retinal angiogenesis and capillary morphogenesis, likely by metabolizing the oxygenated products generated during the oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity).
Cytochrome P450 (CYP450) enzymes are a diverse group of catalysts that contains 57 members in humans. CYPs are usually membrane-bound and are localized to the inner mitochondrial or endoplasmic reticular membrane. CYPs have oxygenase activity.