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Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis

Title
Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis
Authors
Lee S.-K.Park J.-W.Park S.-R.Ahn J.-S.Choi C.-Y.Yoon Y.J.
Ewha Authors
윤여준
SCOPUS Author ID
윤여준scopus
Issue Date
2006
Journal Title
Journal of Microbiology and Biotechnology
ISSN
1017-7825JCR Link
Citation
vol. 16, no. 6, pp. 974 - 978
Indexed
SCIE; SCOPUS; KCI WOS scopus
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, 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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자연과학대학 > 화학·나노과학전공 > Journal papers
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