The catalytic role of aspartate in the active site of glutamate dehydrogenase.

@article{Dean1994TheCR,
  title={The catalytic role of aspartate in the active site of glutamate dehydrogenase.},
  author={Jonathan L. E. Dean and X G Wang and Jan K. Teller and Mark Waugh and K. Linda Britton and Patrick J Baker and Timothy J. Stillman and Stephen R. Martin and David W. Rice and Paul C. Engel},
  journal={The Biochemical journal},
  year={1994},
  volume={301 ( Pt 1)},
  pages={13-6}
}
A putative catalytic aspartyl residue, Asp-165, in the active site of clostridial glutamate dehydrogenase has been replaced with serine by site-directed mutagenesis. The mutant enzyme is efficiently overexpressed in Escherichia coli as a soluble protein and can be successfully purified by the dye-ligand chromatographic procedure normally employed for the wild-type enzyme. By several criteria, including circular dichroism spectrum, sulphydryl reactivity with Ellman's reagent, crystallization and… CONTINUE READING