Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis

Xing-Guo Wang, K. Linda Britton, Timothy J. Stillman, David W. Rice, Paul C. Engel
  • European Journal of Biochemistry, November 2001, Wiley
  • DOI: 10.1046/j.0014-2956.2001.02523.x

Why is it important?

With the first solved structure for GluDH could we now engineer new specificity? Recognition of the substrate's carboxylate sidechain depended on Lys-89 and Ser-380. By changing these to Leu and Ala and also mutating Ala 163 to Gly we eliminate Glu activity and made a dehydrogenase with new specificity for Met and analogous norleucine.

The following have contributed to this page: Professor Paul C Engel