The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b: kinetic and crystallographic studies.

@article{Oikonomakos1995TheBO,
  title={The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b: kinetic and crystallographic studies.},
  author={Nikos G. Oikonomakos and Spyros E Zographos and Louise N. Johnson and Anastassios C Papageorgiou and K Ravi Acharya},
  journal={Journal of molecular biology},
  year={1995},
  volume={254 5},
  pages={
          900-17
        }
}
Kinetic and crystallographic studies have characterized the effect of 2-deoxy-glucose 6-phosphate on the catalytic and structural properties of glycogen phosphorylase b. Previous work on the binding of glucose 6-phosphate, a potent physiological inhibitor of the enzyme, to T state phosphorylase b in the crystal showed that the inhibitor binds at the allosteric site and induces substantial conformational changes that affect the subunit-subunit interface. The hydrogen-bond from the O-2 hydroxyl… CONTINUE READING
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