Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis.

@article{Elleby1999ChangingTE,
  title={Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis.},
  author={B Elleby and Bj{\"o}rn Sj{\"o}blom and Sven Lindskog},
  journal={European journal of biochemistry},
  year={1999},
  volume={262 2},
  pages={516-21}
}
Rates of hydrolysis of 4-, 3-, and 2-nitrophenyl acetate and 4-nitrophenyl propionate catalyzed by wild-type and mutant forms of human carbonic anhydrase II have been measured. The results show that the mutations Tyr7-->Phe and Ala65-->Leu lead to activity enhancements with all the investigated substrates, but there is no significant effect on the specificity. In contrast, some mutations at sequence position 200 have large effects on specificity. For example, while the mutation Thr200-->Gly… CONTINUE READING

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