Article
Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity.
Biochemical and biophysical research communications - 8 Jul 2011
Slavens Kerri D, Brown Teresa R, Barakat Khaldoon A, Cundari Thomas R, Anderson Mary E
Abstract excerpt
It was hypothesized that residues Val44 and Val45 serve as important residues for human glutathione synthetase (hGS) function and stability given their location at the dimer interface of this enzyme. Computational studies suggest that mutation at Val45 has more impact on the structure and stability of hGS than does mutation at Val44. Experimentally, enzymes with mutations at the 44 and or 45 positions of hGS were...
Topics
- Allosteric Regulation
- Catalytic Domain
- Enzyme Stability
- Glutathione Synthase
- Humans
- Isoenzymes
- Mutation
- Protein Multimerization
- Protein Structure, Secondary
- Valine