Cytochrome P450 eryF
Cytochrome P450 eryF | |||||||
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Identifiers | |||||||
Organism | |||||||
Symbol | eryF | ||||||
Alt. symbols | CYP107A1 | ||||||
UniProt | Q00441 | ||||||
Other data | |||||||
EC number | 1.14.15.35 | ||||||
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6-deoxyerythronolide B hydroxylase is an Actinobacteria 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.[1][2] This bacterial enzyme belongs to CYP family CYP107, with the CYP Symbol CYP107A1.[3][4]
References
- ↑ Weber JM, Leung JO, Swanson SJ, Idler KB, McAlpine JB (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.
- ↑ Andersen JF, Hutchinson CR (February 1992). "Characterization of Saccharopolyspora erythraea cytochrome P-450 genes and enzymes, including 6-deoxyerythronolide B hydroxylase". Journal of Bacteriology. 174 (3): 725–35. doi:10.1128/jb.174.3.725-735.1992. PMC 206148. PMID 1732208.
- ↑ Cupp-Vickery JR, Poulos TL (February 1995). "Structure of cytochrome P450eryF involved in erythromycin biosynthesis". Nature Structural Biology. 2 (2): 144–53. doi:10.1038/nsb0295-144. PMID 7749919. S2CID 22536232.
- ↑ Harris DL (September 2002). "Oxidation and electronic state dependence of proton transfer in the enzymatic cycle of cytochrome P450eryF". Journal of Inorganic Biochemistry. 91 (4): 568–85. doi:10.1016/s0162-0134(02)00477-4. PMID 12237223.
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