Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry.

@article{Jhee1998MutationOA,
  title={Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry.},
  author={Kwang Hwan Jhee and Li Hwei Yang and S. A. Ahmed and P. Mcphie and R. David Rowlett and Edith Wilson Miles},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 19},
  pages={
          11417-22
        }
}
To better understand how an enzyme controls cofactor chemistry, we have changed a tryptophan synthase residue that interacts with the pyridine nitrogen of the pyridoxal phosphate cofactor from a neutral Ser (beta-Ser377) to a negatively charged Asp or Glu. The spectroscopic properties of the mutant enzymes are altered and become similar to those of tryptophanase and aspartate aminotransferase, enzymes in which an Asp residue interacts with the pyridine nitrogen of pyridoxal phosphate. The… CONTINUE READING