Article
Some properties of site-specific mutants of human carbonic anhydrase II having active-site residues characterizing carbonic anhydrase III.
European journal of biochemistry - 15 Oct 1991
Ren X L, Jonsson B H, Lindskog S
Abstract excerpt
Four amino acid residues, His64, Asn67, Leu198 and Val207, in the active site of human carbonic anhydrase II, have been replaced by Lys64, Arg67, Phe198 and Ile207, which are characteristic for the muscle-specific, low-activity isoenzyme form, carbonic anhydrase III. The aim of the investigation has been to test if any of these residues, or a combination of them, is important for the low CO2 hydration activity,...
Topics
- Binding Sites
- Carbonic Anhydrases
- Humans
- Hydrogen-Ion Concentration
- Isoenzymes
- Kinetics
- Mutagenesis, Site-Directed
- Mutation
- Spectrometry, Fluorescence