Related Research Articles
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 2E1 is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. This class of enzymes is divided up into a number of subcategories, including CYP1, CYP2, and CYP3, which as a group are largely responsible for the breakdown of foreign compounds in mammals.
Cytochrome P4502C8 (abbreviated CYP2C8), a member of the cytochrome P450 mixed-function oxidase system, is involved in the metabolism of xenobiotics in the body. Cytochrome P4502C8 also possesses epoxygenase activity, i.e. it metabolizes long-chain polyunsaturated fatty acids, e.g. arachidonic acid, eicosapentaenoic acid, docosahexaenoic acid, and Linoleic acid to their biologically active epoxides.
Cytochrome P450 17A1 is an enzyme of the hydroxylase type that in humans is encoded by the CYP17A1 gene on chromosome 10. It is ubiquitously expressed in many tissues and cell types, including the zona reticularis and zona fasciculata of the adrenal cortex as well as gonadal tissues. It has both 17α-hydroxylase and 17,20-lyase activities, and is a key enzyme in the steroidogenic pathway that produces progestins, mineralocorticoids, glucocorticoids, androgens, and estrogens. More specifically, the enzyme acts upon pregnenolone and progesterone to add a hydroxyl (-OH) group at carbon 17 position (C17) of the steroid D ring, or acts upon 17α-hydroxyprogesterone and 17α-hydroxypregnenolone to split the side-chain off the steroid nucleus.
Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an acronym for side-chain cleavage. P450scc is a mitochondrial enzyme that catalyzes conversion of cholesterol to pregnenolone. This is the first reaction in the process of steroidogenesis in all mammalian tissues that specialize in the production of various steroid hormones.
Steroid 21-hydroxylase is an enzyme that hydroxylates steroids at the C21 position and is involved in biosynthesis of aldosterone and cortisol. The enzyme converts progesterone and 17α-hydroxyprogesterone into 11-deoxycorticosterone and 11-deoxycortisol, respectively, within metabolic pathways that ultimately lead to aldosterone and cortisol. Deficiency in the enzyme may cause congenital adrenal hyperplasia.
Cytochrome P450 2C18 is a protein that in humans is encoded by the CYP2C18 gene.
Cytochrome P450 4B1 is a protein that in humans is encoded by the CYP4B1 gene.
Cytochrome P450 4A11 is a protein that in humans is codified by the CYP4A11 gene.
Cytochrome P450 4F8 is a protein that in humans is encoded by the CYP4F8 gene.
The Daf-9 gene encodes a cytochrome p450 enzyme catalysis the generation of dafachronic acid in the worm Caenorhabditis elegans, with the CYP Symbol CYP22A1. After generation, dafachronic acid will binding it's nuclear receptor Daf-12 and has been implicated by Cynthia Kenyon and colleagues related to the formation of Dauer larva.
The Dod-13 gene in the worm Caenorhabditis elegans encoding a cytochrome p450 enzyme, which have steroid hydroxylase activity, with the CYP Symbol CYP35B1. Dod-13 is downstream gene of Daf-16 influenced the lifespan of C. elegans.
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 23, also known as CYP23, is a nematoda cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP23A1 from the Caenorhabditis elegans, is a homolog of the human gene CYP7B1.
Cytochrome P450, family 25, also known as CYP25, is a nematoda cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP25A1 from the Caenorhabditis elegans.
References
- ↑ Nelson, DR (November 1998). "Metazoan cytochrome P450 evolution". Comparative Biochemistry and Physiology. Part C, Pharmacology, Toxicology & Endocrinology. 121 (1–3): 15–22. doi:10.1016/s0742-8413(98)10027-0. PMID 9972448.
- ↑ Wilson, R; Ainscough, R; Anderson, K; Baynes, C; Berks, M; Bonfield, J; Burton, J; Connell, M; Copsey, T; Cooper, J (3 March 1994). "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans". Nature. 368 (6466): 32–8. Bibcode:1994Natur.368...32W. doi:10.1038/368032a0. PMID 7906398. S2CID 21450455.
- ↑ Schäfer, P; Müller, M; Krüger, A; Steinberg, CE; Menzel, R (1 August 2009). "Cytochrome P450-dependent metabolism of PCB52 in the nematode Caenorhabditis elegans". Archives of Biochemistry and Biophysics. 488 (1): 60–8. doi:10.1016/j.abb.2009.06.016. PMID 19563772.
 | This genetics article is a stub. You can help Wikipedia by expanding it. |