Cytochrome P450 eryF

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]

Cytochrome P450 eryF
Identifiers
OrganismSaccharopolyspora erythraea
SymboleryF
Alt. symbolsCYP107A1
UniProtQ00441
Other data
EC number1.14.15.35

References
  1. 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.
  2. 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.
  3. 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.
  4. 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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