CYP107 family

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The evolutionary divergence of the CYP superfamily collected in 1990, CYP107 is the seventh prokaryotic CYP family identified CYP Gene Superfamily.png
The evolutionary divergence of the CYP superfamily collected in 1990, CYP107 is the seventh prokaryotic CYP family identified

Cytochrome P450, family 107, also known as CYP107, is a cytochrome P450 monooxygenase family in bacteria, [1] found to be conserved and highly populated in Streptomyces and Bacillus species. [2] The first gene identified in this family is Cytochrome P450 eryF (CYP107A1) from Saccharopolyspora erythraea . [3] Many enzymes of this family are involved in the synthesis of macrolide antibiotics. [4] 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. [5]

Related Research Articles

<span class="mw-page-title-main">Cytochrome P450</span> Class of enzymes

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.

<span class="mw-page-title-main">CYP2A13</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 2A13 is a protein that in humans is encoded by the CYP2A13 gene.

<span class="mw-page-title-main">CYP20A1</span>

CYP20A1 is a protein which in humans is encoded by the CYP20A1 gene.

<span class="mw-page-title-main">CYP4F11</span> Protein-coding gene in the species Homo sapiens

CYP4F11 is a protein that in humans is encoded by the CYP4F11 gene. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F2, is approximately 16 kb away. Alternatively spliced transcript variants encoding the same protein have been found for this gene.

<span class="mw-page-title-main">CYP4A22</span> Protein-coding gene in the species Homo sapiens

CYP4A22 also known as fatty acid omega-hydroxylase is a protein which in humans is encoded by the CYP4A22 gene.

<span class="mw-page-title-main">CYP2W1</span> Protein-coding gene in the species Homo sapiens

CYP2W1 is a protein that in humans is encoded by the CYP2W1 gene.

<span class="mw-page-title-main">CYP2A7</span> Protein-coding gene in the species Homo sapiens

CYP2A7 is a protein that in humans is encoded by the CYP2A7 gene.

<i>Saccharopolyspora erythraea</i> Species of bacterium

Saccharopolyspora erythraea is a species of actinomycete bacteria within the genus Saccharopolyspora.

6-deoxyerythronolide B hydroxylase is an Actinomycetota Cytochrome P450 enzyme originally from Saccharopolyspora erythraea, catalyzes the 6S-hydroxylate of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) which is the first step of biosynthesis of the macrolide antibiotic erythromycin. This bacterial enzyme belongs to CYP family CYP107, with the CYP Symbol CYP107A1.

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 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 107 subfamily G member 1 is an actinobacterial Cytochrome P450 enzyme originally from Streptomyces rapamycinicus, which catalyzes the oxidation reaction of C27 of pre-rapamycin in the biosynthesis pathway of the macrolide antibiotic rapamycin.

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 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.

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 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 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 154 subfamily C member 3 is an actinobacterial Cytochrome P450 enzyme originally from Streptomyces, which catalyzes the 16α-hydroxylation of various steroids.

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

  1. 1 2 Nebert, DW; Nelson, DR; Coon, MJ; Estabrook, RW; Feyereisen, R; Fujii-Kuriyama, Y; Gonzalez, FJ; Guengerich, FP; Gunsalus, IC; Johnson, EF (January 1991). "The P450 superfamily: update on new sequences, gene mapping, and recommended nomenclature". DNA and Cell Biology. 10 (1): 1–14. doi:10.1089/dna.1991.10.1. PMID   1991046.
  2. Mnguni, FC; Padayachee, T; Chen, W; Gront, D; Yu, JH; Nelson, DR; Syed, K (7 July 2020). "More P450s Are Involved in Secondary Metabolite Biosynthesis in Streptomyces Compared to Bacillus, Cyanobacteria, and Mycobacterium". International Journal of Molecular Sciences. 21 (13): 4814. doi: 10.3390/ijms21134814 . PMC   7369989 . PMID   32646068.
  3. Weber, JM; Leung, JO; Swanson, SJ; Idler, KB; McAlpine, JB (5 April 1991). "An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea". Science. 252 (5002): 114–7. Bibcode:1991Sci...252..114W. doi:10.1126/science.2011746. PMID   2011746.
  4. Kim, V; Lim, YR; Lee, I; Lee, JH; Han, S; Pham, TV; Kim, H; Lee, R; Kang, LW; Kim, D (15 October 2020). "Structural insights into CYP107G1 from rapamycin-producing Streptomyces rapamycinicus". Archives of Biochemistry and Biophysics. 692: 108544. doi:10.1016/j.abb.2020.108544. PMID   32822639.
  5. Nzuza, N; Padayachee, T; Syed, PR; Kryś, JD; Chen, W; Gront, D; Nelson, DR; Syed, K (2021-05-24). "Ancient Bacterial Class Alphaproteobacteria Cytochrome P450 Monooxygenases Can Be Found in Other Bacterial Species". International Journal of Molecular Sciences. 22 (11): 5542. doi: 10.3390/ijms22115542 . PMC   8197338 . PMID   34073951.