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Cytochrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin

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The cytochrome P450 enzyme is one of the most versatile redox proteins and it is responsible for the oxidative metabolism of a wide variety of endogenous and exogenous compounds. The cytochrome P450 gene, CYP105F2, from Streptomyces peucetius was subcloned into the pET-32a(+) vector to overexpress the protein in E. coli BL21 (DE3) pLysS. The expressed enzyme was purified by fast protein liquid chromatography with a DEAE and UNO Q column. A 3D model was constructed based on the known crystallographic structures of cytochrome P450, and comparison with PikC and MoxA signified broad substrate specificity toward structurally diverse compounds. In addition, the in vitro hydroxylation of oleandomycin by purified CYP105F2 observed in liquid chromatography/mass spectrometry and mass/mass spectrometry indicated its flexibility towards alternative polyketides for the structural diversification of the macrolide by post-polyketide synthase hydroxylation.

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The work was supported by a medium-term strategic technology development grant from the Republic of Korea to JKS.

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Correspondence to Jae Kyung Sohng.

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Shrestha, P., Oh, T., Liou, K. et al. Cytochrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin. Appl Microbiol Biotechnol 79, 555 (2008).

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  • Cytochrome P450
  • Heterologous expression
  • Oleandomycin
  • Streptomyces peucetius
  • Substrate flexibility