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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.
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This page is a summary of: Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site‐directed mutagenesis, European Journal of Biochemistry, November 2001, Wiley,
DOI: 10.1046/j.0014-2956.2001.02523.x.
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