Purification and Characterization of Mycobacterium tuberculosis Indole-3-glycerol Phosphate Synthase

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Yanping Yang, Min Zhang, Hongmei Zhang, Jianqiang Lei, Ruiliang Jin, Shengfeng Xu, Jialing Bao, Lu Zhang, and Honghai Wang^*

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai 200433, PR China; fax: 86-21-65648376; E-mail: hhwang@fudan.edu.cn

^* To whom correspondence should be addressed.

Received November 15, 2004; Revision received January 13, 2005

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Indole-3-glycerol phosphate synthase (IGPS) plays an important role in the survival of Mycobacterium tuberculosis. The trpC gene, encoding IGPS, is essential for the growth of M. tuberculosis. It was expressed at the transcriptional level in cultured M. tuberculosis. The recombinant IGPS with an added His-tag was purified. The His-tag was found to have a small effect on the biochemical properties of IGPS. IGPS is a monofunctional enzyme in M. tuberculosis. Recombinant IGPS has considerable beta-pleated sheet and is relatively compact. The enzyme activity is significantly inhibited by denaturants and antibiotics, suggesting that IGPS may be a novel potential drug target of M. tuberculosis.

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KEY WORDS: Mycobacterium tuberculosis, indole-3-glycerol phosphate synthase, enzyme activity, monofunctional enzyme, secondary structure, drug target

DOI: 10.1134/S0006297906130062

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