The amino acid sequence of ribitol dehydrogenase-F, a mutant enzyme with improved xylitol dehydrogenase activity.

@article{HomsiBrandeburgo1999TheAA,
  title={The amino acid sequence of ribitol dehydrogenase-F, a mutant enzyme with improved xylitol dehydrogenase activity.},
  author={Maria In{\^e}s Homsi-Brandeburgo and Marcos Hikari Toyama and S{\'e}rgio Marangoni and Richard J Ward and Jos{\'e} Roberto Giglio and Brian S. Hartley},
  journal={Journal of protein chemistry},
  year={1999},
  volume={18 4},
  pages={
          489-95
        }
}
A mutant ribitol dehydrogenase (RDH-F) was purified from Klebsiella aerogenes strain F which evolved from the wild-type strain A under selective pressure to improve growth on xylitol, a poor substrate used as sole carbon source. The ratio of activities on xylitol (500 mM) and ribitol (50 mM) was 0.154 for RDH-F compared to 0.033 for the wild-type (RDH-A) enzyme. The complete amino acid sequence of RDH-F showed the mutations. Q60 for E60 and V215 for L215 in the single polypeptide chain of 249… CONTINUE READING
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