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Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses. CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted. In almost all of the transformations that they catalyze, P450's affect hydroxylation.
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.
Steroid 21-hydroxylase is a protein that in humans is encoded by the CYP21A2 gene. The protein is an enzyme that hydroxylates steroids at the C21 position on the molecule. Naming conventions for enzymes are based on the substrate acted upon and the chemical process performed. Biochemically, this enzyme is involved in the biosynthesis of the adrenal gland hormones aldosterone and cortisol, which are important in blood pressure regulation, sodium homeostasis and blood sugar control. The enzyme converts progesterone and 17α-hydroxyprogesterone into 11-deoxycorticosterone and 11-deoxycortisol, respectively, within metabolic pathways which in humans ultimately lead to aldosterone and cortisol creation—deficiency in the enzyme may cause congenital adrenal hyperplasia.
Steroid 11β-hydroxylase, also known as steroid 11β-monooxygenase, is a steroid hydroxylase found in the zona glomerulosa and zona fasciculata of the adrenal cortex. Named officially the cytochrome P450 11B1, mitochondrial, it is a protein that in humans is encoded by the CYP11B1 gene. The enzyme is involved in the biosynthesis of adrenal corticosteroids by catalyzing the addition of hydroxyl groups during oxidation reactions.
CYP20A1 is a protein which in humans is encoded by the CYP20A1 gene.
CYP4Z1 is a protein that in humans is encoded by the CYP4Z1 gene.
CYP4F22 is a protein that in humans is encoded by the CYP4F22 gene.
CYP2W1 is a protein that in humans is encoded by the CYP2W1 gene.
Fatty-acid peroxygenase is an enzyme with systematic name fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating). This enzyme catalyses the following chemical reaction
Cytochrome P450 family 19 subfamily A member 1 is a protein that in humans is encoded by the CYP19A1 gene.
Cytochrome P450, family 53, also known as CYP53, is a cytochrome P450 monooxygenase family in fungi related to hydrocarbon assimilation. They are distributed in both Ascomycota and Basidiomycota, could be used as anti-fungal drug target. The first gene identified in this family is the CYP53A1 from Aspergillus niger encoding the Benzoate 4-monooxygenase (bphA).
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 105, also known as CYP105, is a cytochrome P450 monooxygenase family in bacteria, predominantly found in the phylum Actinomycetota and the order Actinomycetales. The first three genes and subfamilies 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.
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 139, also known as CYP139, is a cytochrome P450 monooxygenase family in bacteria. The first gene identified in this family is CYP139A1 from Mycobacterium tuberculosis. Most member of this family belonged to the subfamily A, and involved in the synthesis of secondary metabolites in many mycobacterial species.
Cytochrome P450, family 123, also known as CYP123, is a cytochrome P450 monooxygenase family in bacteria. The first gene in this family to identify function is CYP123A9 from Rhodococcus sp, which catalysis estrone to 16-hydroxyestrone in the estradiol degradation pathway of bacteria.
Cytochrome P450 family 109 subfamily B member 1 is a versatile prokaryote monooxygenase of CYP109 family originally from Bacillus subtilis, its three-dimensional protein crystal structure has been solved.
Cytochrome P450 family 109 subfamily E member 1 is a prokaryote monooxygenase of CYP109 family originally from Bacillus megaterium, could atc as a 24- and 25-Hydroxylase for Cholesterol.
Cytochrome P450, family 197, also known as CYP197, is a cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP197A1 from Bacillus halodurans. CYP197 is one of the only three P450 familis shared in bacteria and archaea, the other two are CYP147 and CYP109. Genes in this family are co-present on archaeal plasmids and chromosomes, implying the plasmid-mediated horizontal gene transfer of these genes from bacteria to archaea.
Cytochrome P450, family 147, also known as CYP147, is a cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP147B1 from Streptomyces avermitilis. CYP147 is one of the only three P450 familis shared in bacteria and archaea, the other two are CYP197 and CYP109.
References
- ↑ Khatri, Y; Hannemann, F; Girhard, M; Kappl, R; Même, A; Ringle, M; Janocha, S; Leize-Wagner, E; Urlacher, VB; Bernhardt, R (January 2013). "Novel family members of CYP109 from Sorangium cellulosum So ce56 exhibit characteristic biochemical and biophysical properties". Biotechnology and Applied Biochemistry. 60 (1): 18–29. doi:10.1002/bab.1087. PMID 23586989.
- ↑ Girhard M, Klaus T, Khatri Y, Bernhardt R, Urlacher VB (June 2010). "Characterization of the versatile monooxygenase CYP109B1 from Bacillus subtilis". Applied Microbiology and Biotechnology. 87 (2): 595–607. doi:10.1007/s00253-010-2472-z. PMID 20186410. S2CID 26265331.
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