Article
Fine tuning of the catalytic properties of carbonic anhydrase. Studies of a Thr200----His variant of human isoenzyme II.
European journal of biochemistry - 20 Jun 1990
Behravan G, Jonsson B H, Lindskog S
Abstract excerpt
The active sites of carbonic anhydrases I contain a unique histidine residue at sequence position 200. To test the hypothesis that His200 is essential for the isoenzyme-specific catalytic and inhibitor-binding properties of carbonic anhydrases I, a variant of human carbonic anhydrase II, having His200 for Thr200, was prepared by oligonucleotide-directed mutagenesis. The variant has a circular dichroic spectrum...
Topics
- Anions
- Binding Sites
- Carbonic Anhydrase Inhibitors
- Carbonic Anhydrases
- Catalysis
- Circular Dichroism
- Enzyme Stability
- Erythrocytes
- Histidine
- Humans
- Hydrogen-Ion Concentration