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.[2][3] The first three genes and subfamilies identified in this family is the herbicide-inducible P-450SU1 (CYP105A1, subfamily A) and P-450SU2 (CYP105B1, subfamily B) from Streptomyces griseolus[4][5] and choP (CYP105C1, subfamily C) from Streptomyces sp's cholesterol oxidase promoter region.[6][1]
Subfamily
edit| Subfamily[7] | first gene identified | Species | REF |
|---|---|---|---|
| A | SU1 (CYP105A1) | Streptomyces griseolus | [4] |
| B | SU2 (CYP105B1) | Streptomyces griseolus | [4] |
| C | choP (CYP105C1) | Streptomyces sp | [6] |
| D | soyC (CYP105D1) | Streptomyces griseus | [8] |
| E | ORF1 (CYP105E1) | Rhodococcus fascians | [9] |
Application
editCYP105 enzymes is widely used in industry, such as the production of pravastatin.[3]
References
edit- ^ a b 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.
- ^ Moody SC, Loveridge EJ (December 2014). "CYP105-diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces". Journal of Applied Microbiology. 117 (6): 1549–63. doi:10.1111/jam.12662. PMC 4265290. PMID 25294646.
- ^ a b Yasuda, K; Sugimoto, H; Hayashi, K; Takita, T; Yasukawa, K; Ohta, M; Kamakura, M; Ikushiro, S; Shiro, Y; Sakaki, T (January 2018). "Protein engineering of CYP105s for their industrial uses". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866 (1): 23–31. doi:10.1016/j.bbapap.2017.05.014. PMID 28583351.
- ^ a b c Omer, CA; Lenstra, R; Litle, PJ; Dean, C; Tepperman, JM; Leto, KJ; Romesser, JA; O'Keefe, DP (June 1990). "Genes for two herbicide-inducible cytochromes P-450 from Streptomyces griseolus". Journal of Bacteriology. 172 (6): 3335–45. doi:10.1128/jb.172.6.3335-3345.1990. PMC 209144. PMID 2345149.
- ^ Hussain, HA; Ward, JM (January 2003). "Enhanced heterologous expression of two Streptomyces griseolus cytochrome P450s and Streptomyces coelicolor ferredoxin reductase as potentially efficient hydroxylation catalysts". Applied and Environmental Microbiology. 69 (1): 373–82. Bibcode:2003ApEnM..69..373H. doi:10.1128/aem.69.1.373-382.2003. PMC 152428. PMID 12514018.
- ^ a b Horii, M; Ishizaki, T; Paik, SY; Manome, T; Murooka, Y (July 1990). "An operon containing the genes for cholesterol oxidase and a cytochrome P-450-like protein from a Streptomyces sp". Journal of Bacteriology. 172 (7): 3644–53. doi:10.1128/jb.172.7.3644-3653.1990. PMC 213338. PMID 2361941.
- ^ Cytochrome P450 Homepage Link
- ^ Trower, MK; Lenstra, R; Omer, C; Buchholz, SE; Sariaslani, FS (August 1992). "Cloning, nucleotide sequence determination and expression of the genes encoding cytochrome P-450soy (soyC) and ferredoxinsoy (soyB) from Streptomyces griseus". Molecular Microbiology. 6 (15): 2125–34. doi:10.1111/j.1365-2958.1992.tb01386.x. PMID 1406253. S2CID 24513397.
- ^ Crespi, M; Vereecke, D; Temmerman, W; Van Montagu, M; Desomer, J (May 1994). "The fas operon of Rhodococcus fascians encodes new genes required for efficient fasciation of host plants". Journal of Bacteriology. 176 (9): 2492–501. doi:10.1128/jb.176.9.2492-2501.1994. PMC 205384. PMID 8169198.
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