We have developed a novel amino acid dehydrogenase (AADH) with broad substrate specificity.[1]  The novel amino acid dehydrogenase was developed from an existing amino acid dehydrogenase scaffold.  Expansion of its substrate specificity was achieved through several rounds of focused mutagenesis.  Application of degenerate codons and a high-throughput screening assay allowed for simplified, rapid evaluation of enzyme variants.  Constraint of mutant library sizes was guided by mechanistic and structural knowledge, ultimately reducing the screening requirements while maintaining an increased chance of generating alternate substrate specificity.  Novel activity was achieved toward a number of compounds while maintaining the enzyme's native enantioselectivity.[1]  M.J. Abrahamson, E. Vazquez-Figueroa, N.B. Woodall, J.C. Moore, A.S. Bommarius, Angew. Chem. Intl. Ed. 2012 , 000; (http://dx.doi.org/10.1002/anie.201107813)

Development of an amine dehydrogenase for synthesis of chiral amines

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.