Activation of carbonic anhydrase II by active-site incorporation of histidine analogs.

@article{Elder2004ActivationOC,
  title={Activation of carbonic anhydrase II by active-site incorporation of histidine analogs.},
  author={Ileana Elder and Shoufa Han and Chingkuang Tu and Heather L Steele and Philip J. Laipis and Ronald E. Viola and David N. Silverman},
  journal={Archives of biochemistry and biophysics},
  year={2004},
  volume={421 2},
  pages={283-9}
}
The hydration of CO2 catalyzed by human carbonic anhydrase II (HCA II) is accompanied by proton transfer from the zinc-bound water of the enzyme to solution. We have replaced the proton shuttling residue His 64 with Ala and placed cysteine residues within the active-site cavity by mutating sites Trp 5, Asn 62, Ile 91, and Phe 131. These mutants were modified at the single inserted cysteine with imidazole analogs to introduce new potential shuttle groups. Catalysis by these modified mutants was… CONTINUE READING

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