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Cytochromes P450 (CYPs) are a superfamily of enzymes containing heme as a cofactor that 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 plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.
Cytochrome P450 1B1 is an enzyme that in humans is encoded by the CYP1B1 gene.
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 7 alpha-hydroxylase also known as cholesterol 7-alpha-monooxygenase or cytochrome P450 7A1 (CYP7A1) is an enzyme that in humans is encoded by the CYP7A1 gene which has an important role in cholesterol metabolism. It is a cytochrome P450 enzyme, which belongs to the oxidoreductase class, and converts cholesterol to 7-alpha-hydroxycholesterol, the first and rate limiting step in bile acid synthesis.
Lanosterol 14α-demethylase (CYP51A1) is 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.
In enzymology, a sterol 14-demethylase (EC 1.14.13.70) is an enzyme that catalyzes the chemical reaction
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.
Cytochrome P450 2F1 is a protein that in humans is encoded by the CYP2F1 gene.
Cytochrome P450 4F12 is a protein that in humans is encoded by the CYP4F12 gene.
CYP39A1 also known as oxysterol 7-α-hydroxylase 2 is a protein that in humans is encoded by the CYP39A1 gene.
CYP26C1 is a protein which in humans is encoded by the CYP26C1gene.
CYP20A1 is a protein which in humans is encoded by the CYP20A1 gene.
CYP8B1 also known as sterol 12-alpha-hydroxylase is a protein which in humans is encoded by the CYP8B1 gene.
CYP4X1 is a protein which in humans is encoded by the CYP4X1 gene.
CYP2W1 is a protein that in humans is encoded by the CYP2W1 gene.
CYP2A7 is a protein that in humans is encoded by the CYP2A7 gene.
ERG5 or Sterol 22-desaturase is a cytochrome P450 enzyme in the ergosterol biosynthesis pathway of fungi Saccharomyces cerevisiae, with the CYP Symbol CYP61A1. CYP61A1 is one of only three P450 enzyme found in baker's yeast, the other two are CYP51F1 and CYP56A1. The ortholog in Schizosaccharomyces pombe, was named CYP61A3 for historical reasons, and is only one of two P450 enzyme found with CYP51F1. ERG5 catalyzes the C22-C23 double bond formation on the sterol side chain of ergostatrienol to convert it into ergostatetraenol, then the C24 double bond of ergostatetrenol will be hydrogenation reduced into ergosterol by ERG4.
Cytochrome P450, family 55, also known as CYP55, is a cytochrome P450 family in fungi supposed to derived from horizontal gene transfer of Actinomycetes CYP105 family member in the ancestor of all Dikarya. The first gene identified in this family is the CYP55A1 from Fusarium oxysporum encoding the NADPH dependent reductase of nitrous oxide.
Cytochrome P450, family 105, also known as CYP105, is a cytochrome P450 monooxygenase family in bacteria, predominantly found in the phylum Actinobacteria and the order Actinomycetales. The first three genes and subfamilys identified in this family is the herbicide-inducible P-450SU1 and P-450SU2 from Streptomyces griseolus and choP from Streptomyces sp 's cholesterol oxidase promoter region.
References
- ↑ Kelly, SL; Kelly, DE (19 February 2013). "Microbial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us?". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368 (1612): 20120476. doi:10.1098/rstb.2012.0476. PMC 3538425 . PMID 23297358.
- ↑ Morikawa T, Mizutani M, Aoki N, Watanabe B, Saga H, Saito S, et al. (April 2006). "Cytochrome P450 CYP710A encodes the sterol C-22 desaturase in Arabidopsis and tomato". The Plant Cell. 18 (4): 1008–22. doi:10.1105/tpc.105.036012. PMC 1425849 . PMID 16531502.
- ↑ Chen W, Lee MK, Jefcoate C, Kim SC, Chen F, Yu JH (June 2014). "Fungal cytochrome p450 monooxygenases: their distribution, structure, functions, family expansion, and evolutionary origin". Genome Biology and Evolution. 6 (7): 1620–34. doi:10.1093/gbe/evu132. PMC 4122930 . PMID 24966179.
- ↑ Nelson DR (January 2018). "Cytochrome P450 diversity in the tree of life". Biochimica et Biophysica Acta. Proteins and Proteomics. 1866 (1): 141–154. doi:10.1016/j.bbapap.2017.05.003. PMC 5681887 . PMID 28502748.
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