Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Hydroxylation of Indole by PikC Cytochrome P450 from Streptomyces venezuelae and Engineering Its Catalytic Activity by Site-Directed Mutagenesis

  • Lee Sang-Kil (School of Chemical and Biological Engineering, Seoul National University) ;
  • Park Je-Won (Division of Nano Sciences and Department of Chemistry, Ewha Womans University) ;
  • Park Sung-Ryeol (Division of Nano Sciences and Department of Chemistry, Ewha Womans University) ;
  • Ahn Jong-Seog (Laboratory of Cellular Signaling Modulator, Korea Research Institute of Bioscience and Biotechnology) ;
  • Choi Cha-Yong (School of Chemical and Biological Engineering, Seoul National University) ;
  • Yoon Yeo-Joon (Division of Nano Sciences and Department of Chemistry, Ewha Womans University)
  • Published : 2006.06.01
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Abstract

The cytochrome P450 monooxygenase from the pikromycin biosynthetic gene cluster in Streptomyces venezuelae, known as PikC, was observed to hydroxylate the unnatural substrate indole to indigo. Furthermore, the site-directed mutagenesis of PikC monooxygenase led to the mutant enzyme F171Q, in which Phe171 was altered to Gln, with enhanced activity for the hydroxylation of indole. From enzyme kinetic studies, F171Q showed an approximately five-fold higher catalytic efficiency compared with the wild-type PikC. Therefore, these results demonstrate the promising application of P450s originating from Streptomyces, normally involved in polyketide biosynthesis, to generate a diverse array of other industrially useful compounds.

Keywords

References

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