A marriage full of surprises: forty-five years living with glutamate dehydrogenase.

@article{Engel2011AMF,
  title={A marriage full of surprises: forty-five years living with glutamate dehydrogenase.},
  author={Paul C. Engel},
  journal={Neurochemistry international},
  year={2011},
  volume={59 4},
  pages={489-94}
}
Detailed kinetic studies of bovine glutamate dehydrogenase [GDH] from the 1960s revealed complexities that remain to be fully explained. In the absence of heterotropic nucleotide regulators the enzyme follows a random pathway of substrate addition but saturation with ADP enforces a compulsory-order mechanism in which glutamate is the leading substrate. The rate dependence on NAD(P)(+) concentration is complex and is probably only partly explained by negative binding cooperativity. Bovine GDH… CONTINUE READING