Article
Site-directed mutations of arginine 65 at the periphery of the active site cleft of yeast 3-phosphoglycerate kinase enhance the catalytic activity and eliminate anion-dependent activation.
Protein engineering - 1 Dec 1991
Sherman M A, Dean S A, Mathiowetz A M, Mas M T
Abstract excerpt
The function of arginine 65, a conserved residue located at the periphery of the active site cleft in yeast 3-phosphoglycerate kinase (PGK), has been investigated by site-directed mutagenesis. Mutant enzymes with glutamine, serine and alanine at position 65 all have very similar kinetic properties. The maximum velocities, determined in the absence of sulfate anion, are approximately 100% higher than the Vmax of...
Topics
- Anions
- Arginine
- Base Sequence
- Binding Sites
- Diphosphoglyceric Acids
- Enzyme Activation
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed