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The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion where it plays a critical role in cellular respiration. It transfers electrons between Complexes III and IV. Cytochrome c is highly water-soluble, unlike other cytochromes. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It also plays a major role in cell apoptosis. In humans, cytochrome c is encoded by the CYCS gene.
Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function 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.
The inner mitochondrial membrane (IMM) is the mitochondrial membrane which separates the mitochondrial matrix from the intermembrane space.
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.
CYP27A1 is a gene encoding a cytochrome P450 oxidase, and is commonly known as sterol 27-hydroxylase. This enzyme is located in many different tissues where it is found within the mitochondria. It is most prominently involved in the biosynthesis of bile acids.
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.
In enzymology, a cholestanetriol 26-monooxygenase (EC 1.14.13.15) is an enzyme that catalyzes the chemical reaction
Adrenal ferredoxin is a protein that in humans is encoded by the FDX1 gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.
Adrenodoxin reductase, was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.
CYP8B1 also known as sterol 12-alpha-hydroxylase is a protein which in humans is encoded by the CYP8B1 gene.
Adrenodoxin-NADP+ reductase (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, ADR, NADPH:adrenal ferredoxin oxidoreductase) is an enzyme with systematic name adrendoxin:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction
Cytochrome P450, family 107, also known as CYP107, is a cytochrome P450 monooxygenase family in bacteria, found to be conserved and highly populated in Streptomyces and Bacillus species. The first gene identified in this family is Cytochrome P450 eryF (CYP107A1) from Saccharopolyspora erythraea. Many enzymes of this family are involved in the synthesis of macrolide antibiotics. The members of this family are widely distributed in Alphaproteobacteria, cyanobacterial, Mycobacterium, Bacillota, and Streptomyces species, which may be due to horizontal gene transfer driven by selection pressure.
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 10, also known as CYP10, is a cytochrome P450 family found in Lophotrochozoa belongs to Mitochondrial clan CYPs, which is located in the inner membrane of mitochondria(IMM). The first gene identified in this family is the CYP10A1 from the Lymnaea stagnalis, which is highly expressed in the female gonadotropic hormone producing dorsal bodies.
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 18, also known as CYP18, is an animal cytochrome P450 family found in insect genomes. It is involved in insecticide resistance. The first member gene identified was CYP18A1, from a Drosophila melanogaster fly, acting as a dimethylnitrosamine demethylase.
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 15, also known as CYP15, is an animal cytochrome P450 family found in insect genome, involved in juvenile hormone biosynthesis. The first gene identified in this family is the DpCYP15A1 from the Diploptera punctata, encodes an epoxidase of methyl farnesoate, a precursor of juvenile hormone, alone with its ortholog TcCYP15A1 in Tribolium castaneum.
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.
Cytochrome P450, family 27, also known as CYP27, is a Deuterostome cytochrome P450 monooxygenase family found in human genome. This family belongs to Mitochondrial clan CYPs, which is located in the inner membrane of mitochondria(IMM). There are three members in the human genome, CYP27A1, CYP27B1 and CYP27C1, and an ortholog CYP27F1 in sea urchins, Strongylocentrotus purpuratus.
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.
- ↑ Tijet, N; Helvig, C; Feyereisen, R (10 January 2001). "The cytochrome P450 gene superfamily in Drosophila melanogaster: annotation, intron-exon organization and phylogeny". Gene. 262 (1–2): 189–98. doi:10.1016/s0378-1119(00)00533-3. PMID 11179683.
- 1 2 Guzov, VM; Unnithan, GC; Chernogolov, AA; Feyereisen, R (15 November 1998). "CYP12A1, a mitochondrial cytochrome P450 from the house fly". Archives of Biochemistry and Biophysics. 359 (2): 231–40. doi:10.1006/abbi.1998.0901. PMID 9808765.
- ↑ Eggertsen, G; Olin, M; Andersson, U; Ishida, H; Kubota, S; Hellman, U; Okuda, KI; Björkhem, I (13 December 1996). "Molecular cloning and expression of rabbit sterol 12alpha-hydroxylase". The Journal of Biological Chemistry. 271 (50): 32269–75. doi: 10.1074/jbc.271.50.32269 . PMID 8943286. S2CID 84628848.
- ↑ Nelson, DR (2006). "Cytochrome P450 Nomenclature, 2004". Cytochrome P450 Protocols. Methods in Molecular Biology. Vol. 320. pp. 1–10. doi:10.1385/1-59259-998-2:1. ISBN 1-59259-998-2. PMID 16719369.
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