Article
Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I.
European journal of biochemistry - 1 May 1995
Engstrand C, Jonsson B H, Lindskog S
Abstract excerpt
Three isozyme-specific residues in the active site of human carbonic anhydrase I, Val62, His67, and His200, have been changed by site-directed mutagenesis to their counterparts in human carbonic anhydrase II, Asn62, Asn67, and Thr200. A double mutant, containing Asn62 and Asn67, and a triple muta...
Topics
- Amino Acids
- Binding Sites
- Carbonic Anhydrase Inhibitors
- Carbonic Anhydrases
- Catalysis
- Humans
- Isoenzymes
- Kinetics
- Magnetic Resonance Spectroscopy
- Mutagenesis, Site-Directed
- Mutation
- Structure-Activity Relationship
