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Cytochromes P450 (CYPs) are a superfamily of enzymes containing heme as a cofactor that functions as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Estabrook, Cooper, and Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.
Cytochrome P450 3A4 is an important enzyme in the body, mainly found in the liver and in the intestine. It oxidizes small foreign organic molecules (xenobiotics), such as toxins or drugs, so that they can be removed from the body. It is highly homologous to CYP3A5, another important CYP3A enzyme.
Cytochrome P450 2A6 is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. CYP2A6 is the primary enzyme responsible for the oxidation of nicotine and cotinine. It is also involved in the metabolism of several pharmaceuticals, carcinogens, and a number of coumarin-type alkaloids. CYP2A6 is the only enzyme in the human body that appreciably catalyzes the 7-hydroxylation of coumarin, such that the formation of the product of this reaction, 7-hydroxycoumarin, is used as a probe for CYP2A6 activity.
Lanosterol 14α-demethylase (CYP51A1) is the animal version of a cytochrome P450 enzyme that is involved in the conversion of lanosterol to 4,4-dimethylcholesta-8(9),14,24-trien-3β-ol. The cytochrome P450 isoenzymes are a conserved group of proteins that serve as key players in the metabolism of organic substances and the biosynthesis of important steroids, lipids, and vitamins in eukaryotes. As a member of this family, lanosterol 14α-demethylase is responsible for an essential step in the biosynthesis of sterols. In particular, this protein catalyzes the removal of the C-14α-methyl group from lanosterol. This demethylation step is regarded as the initial checkpoint in the transformation of lanosterol to other sterols that are widely used within the cell.
Cytochrome P450 3A5 is a protein that in humans is encoded by the CYP3A5 gene.
Cytochrome P450, family 3, subfamily A, also known as CYP3A, is a human gene locus. A homologous locus is found in mice.
Cytochrome P450 2A13 is a protein that in humans is encoded by the CYP2A13 gene.
Cytochrome P450 3A43 is a protein that in humans is encoded by the CYP3A43 gene.
Leukotriene-B(4) omega-hydroxylase 2 is an enzyme that in humans is encoded by the CYP4F3 gene. CYP4F3 encodes two distinct enzymes, CYP4F3A and CYP4F3B, which originate from the alternative splicing of a single pre-mRNA precursor molecule; selection of either isoform is tissue-specific with CYP3F3A being expressed mostly in leukocytes and CYP4F3B mostly in the liver.
CYP4Z1 is a protein that in humans is encoded by the CYP4Z1 gene.
Cytochrome P450 BM3 is a Prokaryote Cytochrome P450 enzyme originally from Bacillus megaterium catalyzes the hydroxylation of several long-chain fatty acids at the ω–1 through ω–3 positions. This bacterial enzyme belongs to CYP family CYP102, with the CYP Symbol CYP102A1.This CYP family constitutes a natural fusion between the CYP domain and an NADPH-dependent cytochrome P450 reductase.
Cytochrome P450, family 52, also known as CYP52, is a cytochrome P450 family in fungi participate in the assimilation of alkanes and fatty acids, which the most ancient function was the oxidation of C4-C11 alkanes. The first gene identified in this family is the alkane-inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis, with CYP Symbol CYP52A1.
Cytochrome P450, family 710, also known as CYP710, is a plant cytochrome P450 monooxygenase family, the proteins encoded by its family members are mainly sterol 22-desaturase, which was widely distributed in plants, and take participate in Phytosteroidogenesis. CYP710 family is considered to be the plant orthologous of fungi CYP61 family, which is lost in animal. The CYP61/CYP710 ancestor gene diverged from a gene duplication of ancestor CYP51 in early eukaryotes
Cytochrome P450, family 11, also known as CYP11, is a chordate cytochrome P450 monooxygenase family. This family contains many enzymes involved in steroidogenesis, such as Cholesterol side-chain cleavage enzyme (CYP11A1), Steroid 11β-hydroxylase (CYP11B1) and Aldosterone synthase (CYP11B2). CYP11 can be divided into A to E five subfamilies, and CYP11A are the ohonologues to CYP11C, which duplicated during 2R event, and the tetrapod's CYP11B evolved from CYP11C of its fish ancestors, CYP11D and F found in amphioxus. These are not the typical CYP subfamilies, which share at least 40% amino acid identity, members between CYP11A and B subfamily are only 37.5-38.8% identical, and the CYP11D and E genes seen in modern lancelet is 39% identical to catfish CYP11A1.
Cytochrome P450, family 16, also known as CYP16, is an animal cytochrome P450 monooxygenase family. This family was the last vertebrate CYP family recognized, and is absent from the mammal and zebrafish genome, but found in other fish and many invertebrates including some very old branches, such as Trichoplax and Oscarella carmela. Synteny mapping of CYP16 family members showing linkages to CYP26 family members, means the tetrapod's CYP26 may evolved from CYP16 of fish.
Cytochrome P450, family 9, also known as CYP9, is a cytochrome P450 family found in Insect genome, CYP9 and insect CYP6 family belong to the same clan as mammalian CYP3 and CYP5 families. The first gene identified in this family is the CYP9A1 from the Heliothis virescens, which is involved in thiodicarb insecticide resistance. Subfamily CYP9A in Lepidopteran play important roles in insecticide resistance, can metabolize esfenvalerate efficiently.
Cytochrome P450, family 6, also known as CYP6, is a cytochrome P450 family found in Insect genome. CYP6 and CYP9, another insect CYP family, belong to the same clan as mammalian CYP3 and CYP5 families.
Cytochrome P450, family 12, also known as CYP12, is a cytochrome P450 family found in insect genome belongs to Mitochondrial clan CYPs, which is located in the inner membrane of mitochondria(IMM). The first gene identified in this family is the CYP12A1 from the Musca domestica, which is involved in insecticide resistance. CYP12A1 protein localization in mitochondria by immunohistochemistry and absolute dependence on mitochondrial electron donors adrenodoxin reductase and adrenodoxin.
Cytochrome P450, family 13, also known as CYP13, is a nematoda cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP13A1 from the Caenorhabditis elegans.
Cytochrome P450, family 26, also known as CYP26, is an mammal cytochrome P450 monooxygenase family found in human genome. There are three members in the human genome, CYP26A1, CYP26B1 and CYP26C1. Synteny mapping of CYP26 family members showing linkages to CYP16 family members of many invertebrates, means the tetrapod's CYP26 may evolved from CYP16 of fish.
References
- ↑ Teunissen, Y; Geraerts, WP; van Heerikhuizen, H; Planta, RJ; Joosse, J (August 1992). "Molecular cloning of a cDNA encoding a member of a novel cytochrome P450 family in the mollusc Lymnaea stagnalis". Journal of Biochemistry. 112 (2): 249–52. doi:10.1093/oxfordjournals.jbchem.a123885. PMID 1400265.
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