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Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis
- Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis
- Lee S.-K.; Park J.-W.; Park S.-R.; Ahn J.-S.; Choi C.-Y.; Yoon Y.J.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Journal of Microbiology and Biotechnology
- Journal of Microbiology and Biotechnology vol. 16, no. 6, pp. 974 - 978
- SCIE; SCOPUS; KCI
- Document Type
- 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, norinally involved in polyketide biosynthesis, to generate a diverse array of other industrially useful compounds. © The Korean Society for Microbiology and Biotechnology.
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