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

Sang Kil Lee, Je Won Park, Sung Ryeol Park, Jong Seog Ahn, Cha Yong Choi, Yeo Joon Yoon

Research output: Contribution to journalArticle

11 Citations (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.

Original languageEnglish
Pages (from-to)974-978
Number of pages5
JournalJournal of microbiology and biotechnology
Volume16
Issue number6
Publication statusPublished - 2006 Jun 1
Externally publishedYes

Fingerprint

Streptomyces
Hydroxylation
Mixed Function Oxygenases
Site-Directed Mutagenesis
Cytochrome P-450 Enzyme System
Catalytic Domain
Indigo Carmine
Polyketides
Enzymes
Multigene Family
indole
picromycin

Keywords

  • Cytochrome P450 monooxygenase
  • Indigo
  • Indole-hydroxylating
  • PikC
  • Site-directed mutagenesis
  • Streptomyces venezuelae

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis. / Lee, Sang Kil; Park, Je Won; Park, Sung Ryeol; Ahn, Jong Seog; Choi, Cha Yong; Yoon, Yeo Joon.

In: Journal of microbiology and biotechnology, Vol. 16, No. 6, 01.06.2006, p. 974-978.

Research output: Contribution to journalArticle

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AU - Choi, Cha Yong

AU - Yoon, Yeo Joon

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AB - 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.

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