Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase.

@article{Smith1994MutationsAT,
  title={Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase.},
  author={A. A. Smith and D. Carlow and R. Wolfenden and S. Short},
  journal={Biochemistry},
  year={1994},
  volume={33 21},
  pages={
          6468-74
        }
}
Cytidine deaminase from Escherichia coli contains 1 mol of tightly bound zinc per enzyme subunit (Yang, C., Carlow, D., Wolfenden, R., & Short, S.A. (1992) Biochemistry 31, 4168-4174). When the metal liganding residues Cys-129 and Cys-132 were replaced by Ala, and His-102 was replaced by Ala, Asn, or Gln, deaminase activities of cell extracts containing these mutant enzymes were decreased by several orders of magnitude relative to that of the wild-type enzyme. After purification, each mutant… Expand
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TLDR
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