Article
Ligand-induced conformational changes in wild-type and mutant yeast pyruvate kinase.
Protein engineering - 1 Dec 1996
Collins R A, Kelly S M, Price N C, Fothergill-Gilmore L A, Muirhead H
Abstract excerpt
A mutant form of pyruvate kinase in which serine 384 has been mutated to proline has been engineered in the yeast Saccharomyces cerevisiae. Residue 384 is located in a helix in a subunit interface of the tetrameric enzyme, and the mutation was anticipated to alter the conformation of the helix an...
Topics
- Adenosine Diphosphate
- Allosteric Regulation
- Cations
- Circular Dichroism
- Ethylmaleimide
- Fructosediphosphates
- Hot Temperature
- Hydrogen-Ion Concentration
- Ligands
- Mutation
- Phosphoenolpyruvate
- Protein Conformation
- Protein Denaturation
- Protein Engineering
- Pyruvate Kinase
- Saccharomyces cerevisiae
- Spectrometry, Fluorescence
- Sulfhydryl Reagents