Influence of amino acid replacement at position 198 on catalytic properties of zinc-bound water in human carbonic anhydrase III.

@article{Lograsso1993InfluenceOA,
  title={Influence of amino acid replacement at position 198 on catalytic properties of zinc-bound water in human carbonic anhydrase III.},
  author={Philip V Lograsso and Chingkuang Tu and Xiaochun Chen and Shin Taoka and Philip J. Laipis and David N. Silverman},
  journal={Biochemistry},
  year={1993},
  volume={32 22},
  pages={5786-91}
}
Carbonic anhydrase III, found predominantly in skeletal muscle, is the least efficient of the mammalian carbonic anhydrases in catalyzing the hydration of CO2. Phenylalanine-198 is located on the hydrophobic side of the active-site cavity with its phenyl ring in the proximity of the catalytically active zinc-bound water. We replaced phenylalanine-198 in human carbonic anhydrase III with seven other amino acids (Ala, Asn, Asp, His, Leu, Tyr, Val) using site-directed mutagenesis. The catalytic… CONTINUE READING