Novel substrates of a ribose-5-phosphate isomerase from Clostridium thermocellum.

@article{Yoon2009NovelSO,
  title={Novel substrates of a ribose-5-phosphate isomerase from Clostridium thermocellum.},
  author={Ran-Young Yoon and Soo-Jin Yeom and Hye-Jung Kim and Deok-Kun Oh},
  journal={Journal of biotechnology},
  year={2009},
  volume={139 1},
  pages={26-32}
}
A substrate specificity study of the recombinant D-ribose-5-phosphate isomerase (RpiB) from Clostridium thermocellum was performed. Among all aldopentoses and aldohexoses, the RpiB enzyme displayed activity with L-talose, D-ribose, D-allose, L-allose, L-ribose, and D-talose in decreasing order. The products released were L-tagatose, D-ribulose, D-psicose, L-psicose, L-ribulose, and D-tagatose, respectively. The enzyme showed specificity for aldose substrates possessing hydroxyl groups oriented… CONTINUE READING
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