전체메뉴
Advanced Search +

JMB Journal of Microbiolog and Biotechnology

QR Code QR Code

Hydroxylation of Indole by PikC Cytochrome P450 from Streptomyces venezuelae and Engineering Its Catalytic Activity by Site-Directed Mutagenesis

Lee, Sang-Kil , Je-Won Park 1, Sung-Ryeol Park 1, Jong-Seog Ahn 2, Cha-Yong Choi 3 and Yeo Joon Yoon 3*

1School of Chemical and Biological Engineering, Seoul National University, Seoul 151-742, Korea, 1Division of Nano Sciences and Department of Chemistry, Ewha Womans University, Seoul 120-750, Korea, 2Laboratory of Cellular Signaling Modulator, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-333, Korea, 3School of Chemical and Biological Engineering, Seoul National University, Seoul 151-742, Korea

J. Microbiol. Biotechnol. 2006; 16(6): 974-978

Published June 28, 2006

Copyright © The Korean Society for Microbiology and Biotechnology.

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, normally involved in polyketide biosynthesis, to generate a diverse array of other industrially useful compounds.

Keywords

PikC cytochrome P450 monooxygenase, Streptomyces venezuelae, indigo, indole-hydroxylating, sitedirected mutagenesis

Related articles in JMB

More Related Articles

Article

J. Microbiol. Biotechnol. 2006; 16(6): 974-978

Published online June 28, 2006

Copyright © The Korean Society for Microbiology and Biotechnology.

Hydroxylation of Indole by PikC Cytochrome P450 from Streptomyces venezuelae and Engineering Its Catalytic Activity by Site-Directed Mutagenesis

Lee, Sang-Kil , Je-Won Park 1, Sung-Ryeol Park 1, Jong-Seog Ahn 2, Cha-Yong Choi 3 and Yeo Joon Yoon 3*

1School of Chemical and Biological Engineering, Seoul National University, Seoul 151-742, Korea, 1Division of Nano Sciences and Department of Chemistry, Ewha Womans University, Seoul 120-750, Korea, 2Laboratory of Cellular Signaling Modulator, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-333, Korea, 3School of Chemical and Biological Engineering, Seoul National University, Seoul 151-742, Korea

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, normally involved in polyketide biosynthesis, to generate a diverse array of other industrially useful compounds.

Keywords: PikC cytochrome P450 monooxygenase, Streptomyces venezuelae, indigo, indole-hydroxylating, sitedirected mutagenesis