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

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Title
Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis
Author(s)
S K Lee; J W Park; S R Park; Jong Seog Ahn; C Y Choi; Y J Yoon
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 16, no. 6, pp. 974-978
Publication Year
2006
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.
Keyword
cytochrome P450 monooxygenaseindigoindole-hydroxylatingPikCsite-directed mutagenesisstreptomyces venezuelae
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
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