Characterization of the structure and properties of the His 62-->Ala and Arg 38-->Ala mutants of yeast phosphoglycerate kinase: an investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR.

@article{Sherman1992CharacterizationOT,
  title={Characterization of the structure and properties of the His 62-->Ala and Arg 38-->Ala mutants of yeast phosphoglycerate kinase: an investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR.},
  author={Mark A. Sherman and Wayne J Fairbrother and Mar{\'i}a Torras Mas},
  journal={Protein science : a publication of the Protein Society},
  year={1992},
  volume={1 6},
  pages={
          752-60
        }
}
The role of two "basic patch" residues, Arg-38 and His-62, in the catalytic function and anion-dependent activation of yeast 3-phosphoglycerate kinase (PGK) was investigated by site-directed mutagenesis. Steady-state kinetics and NMR experiments were conducted to characterize the functional properties and structural integrity of the R38A and H62A mutants. The results of these studies, in combination with earlier mutagenesis experiments, suggest that Arg-38 is the only catalytically essential… CONTINUE READING
BETA

Similar Papers

Topics from this paper.

Citations

Publications citing this paper.