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  • Title: Substrate specificity of ribose-5-phosphate isomerases from Clostridium difficile and Thermotoga maritima.
    Author: Yeom SJ, Kim BN, Park CS, Oh DK.
    Journal: Biotechnol Lett; 2010 Jun; 32(6):829-35. PubMed ID: 20155483.
    Abstract:
    The activity of ribose-5-phosphate isomerases (RpiB) from Clostridium difficile for D-ribose isomerization was optimal at pH 7.5 and 40 degrees C, while that from Thermotoga maritima for L-talose isomerization was optimal at pH 8.0 and 70 degrees 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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