A single amino acid substitution changes ribonuclease 4 from a uridine-specific to a cytidine-specific enzyme.

@article{Hofsteenge1998ASA,
  title={A single amino acid substitution changes ribonuclease 4 from a uridine-specific to a cytidine-specific enzyme.},
  author={J. A. Hofsteenge and Charles F. Moldow and Albertina Vicentini and Ottilie Zelenko and Z Jarai-Kote and Ulrich Neumann},
  journal={Biochemistry},
  year={1998},
  volume={37 26},
  pages={
          9250-7
        }
}
The structural features underlying the strong uridine specificity of ribonuclease 4 (RNase 4) are largely unknown. It has been hypothesized that the negatively charged alpha-carboxylate is close to the pyrimidine binding pocket, due to a unique C-terminal deletion. This would suppress the cleavage of cytidine-containing substrates [Zhou, H.-M., and Strydom, D. J. (1993) Eur. J. Biochem. 217, 401-410]. Replacement of the alpha-carboxylate by an alpha-carboxamide in a fragment complementation… CONTINUE READING
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