Article
Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase.
Science (New York, N.Y.) - 31 Aug 1990
Dean A M, Koshland D E
Abstract excerpt
The isocitrate dehydrogenase of Escherichia coli is regulated by covalent modification at the active site rather than, as expected, at an allosteric site. As a means of evaluating the mechanism of regulation, the kinetics of the substrate, 2R,3S-isocitrate, and a substrate analog, 2R-malate, were...
Topics
- Allosteric Site
- Amino Acid Sequence
- Binding Sites
- Escherichia coli
- Isocitrate Dehydrogenase
- Models, Molecular
- Mutation
- Protein Conformation