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Substrate specificity of ribose-5-phosphate isomerases from Clostridium difficile and Thermotoga maritima

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Abstract

The activity of ribose-5-phosphate isomerases (RpiB) from Clostridium difficile for d-ribose isomerization was optimal at pH 7.5 and 40°C, while that from Thermotoga maritima for l-talose isomerization was optimal at pH 8.0 and 70°C. C. difficile RpiB exhibited activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as d-ribose, d-allose, l-talose, l-lyxose, d-gulose, and l-mannose. In contrast, T. maritima RpiB displayed activity only with aldose substrates possessing hydroxyl groups configured the same direction at the C2, C3, and C4 positions, such as the d- and l-forms of ribose, talose, and allose.

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Acknowledgments

This study was supported by a grant (R0A-2007-000-20015-0) from the National Research Lab. Program, Ministry of Education, Science and Technology.

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Authors and Affiliations

  1. Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul, 143-701, South Korea

    Soo-Jin Yeom, Bi-Na Kim, Chang-Su Park & Deok-Kun Oh

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  1. Soo-Jin Yeom
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  2. Bi-Na Kim
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  3. Chang-Su Park
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Correspondence to Deok-Kun Oh.

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Yeom, SJ., Kim, BN., Park, CS. et al. Substrate specificity of ribose-5-phosphate isomerases from Clostridium difficile and Thermotoga maritima . Biotechnol Lett 32, 829–835 (2010). https://doi.org/10.1007/s10529-010-0224-x

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  • DOI: https://doi.org/10.1007/s10529-010-0224-x

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