Article
Active-site mutants altering the cooperativity of E. coli phosphofructokinase.
Nature - 8 Feb 1990
Berger S A, Evans P R
Abstract excerpt
Crystal structures of the high- and low-activity states of the allosteric enzyme phosphofructokinase implicate three arginines in substrate binding, catalysis and cooperativity. Arginines 162 and 243 reach into the active site from an adjacent subunit and interact with the cooperative substrate f...
Topics
- Adenosine Triphosphate
- Allosteric Regulation
- Arginine
- Binding Sites
- Escherichia coli
- Fructosephosphates
- Guanosine Diphosphate
- Kinetics
- Molecular Structure
- Mutation
- Phosphofructokinase-1
- Protein Conformation
- Structure-Activity Relationship