Article
Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala.
Protein engineering - 1 Feb 1996
Tougard P, Le T H, Minard P, Desmadril M, Yon J M, Bizebard T, Lebras G, Dumas C
Abstract excerpt
A pathological variant of human phosphoglycerate kinase, phosphoglycerate kinase-Uppsala, associated with chronic nonspherocytic hemolytic anemia has been found to differ from the normal enzyme by substitution of an arginine at position 206 (corresponding to position 203 in yeast) by a proline. I...
Topics
- Circular Dichroism
- Crystallography, X-Ray
- Enzyme Stability
- Guanidine
- Guanidines
- Kinetics
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Phosphoglycerate Kinase
- Protein Conformation
- Protein Folding
- Sulfates
- Yeasts