Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200.

Abstract

The active-site residue Thr200 in human carbonic anhydrase II has been replaced by several different amino acids by site-directed mutagenesis. The CO2 hydration and 4-nitrophenyl acetate hydrolase activities of these variants have been measured, as well as inhibition by the monovalent anion, SCN-. The results show that the replacement of Thr200 with Ser or… (More)

Topics

Cite this paper

@article{Behravan1991FineTO, title={Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200.}, author={G Behravan and Bo H Jonsson and Stefan Lindskog}, journal={European journal of biochemistry}, year={1991}, volume={195 2}, pages={393-6} }