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

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11 Citations (Scopus)


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
Issue number6
Publication statusPublished - 2006 Jun 1
Externally publishedYes



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

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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