A study of the hinge-bending mechanism of yeast 3-phosphoglycerate kinase.

@article{Dryden1992ASO,
  title={A study of the hinge-bending mechanism of yeast 3-phosphoglycerate kinase.},
  author={David T. F. Dryden and P. G. Varley and Roger H. Pain},
  journal={European journal of biochemistry},
  year={1992},
  volume={208 1},
  pages={
          115-23
        }
}
  • David T. F. Dryden, P. G. Varley, Roger H. Pain
  • Published in
    European journal of…
    1992
  • Medicine, Chemistry
  • The hinge-bending mechanism proposed as part of the catalytic mechanism for phosphoglycerate kinase (PGK) has been investigated using yeast PGK and the site-directed mutant [H388Q]PGK, where His388 is replaced by Gln. The emission and quenching of fluorescence, supported by the aromatic CD band, show that the mutation in the waist region affects the tryptophan environment in the C-terminal domain. The mutant is also less stable to guanidine denaturation and less cooperative in its unfolding… CONTINUE READING

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