Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase.

@article{Thompson2005VmaxRT,
  title={Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase.},
  author={James R. Thompson and Jessica K. Bell and Judy Bratt and Gregory A Grant and Leonard J. Banaszak},
  journal={Biochemistry},
  year={2005},
  volume={44 15},
  pages={5763-73}
}
An active conformation of phosphoglycerate dehydrogenase (PGDH) from Escherichia coli has been obtained using X-ray crystallography. The X-ray crystal structure is used to examine the potential intermediates for V(max) regulation, for the redox reaction, and for cooperative effects of serine binding. The crystal structure at 2.2 A resolution contains bound NAD(+) cofactor, either sulfate or phosphate anions, and alpha-ketoglutarate, a nonphysiological substrate. A PGDH subunit is formed from… CONTINUE READING

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