Substrate Specificity Change of a Dehydrogenase

Monday, October 17, 2011: 4:35 PM
M100 H (Minneapolis Convention Center)
Michael J. Abrahamson and Andreas S. Bommarius, School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA

Biocatalysts are increasingly used in industry to create enantiomerically pure compounds.  Enantiomeric compounds have a broad range of uses including an utmost importance in pharmaceuticals.  Biocatalysis employs enzymes to produce enantiomerically pure compounds circumventing the difficulties of current production methods.  Contemporary methods of protein engineering, such as applying rational design guided by mechanistic and structural knowledge, have greatly increased the ability to create novel enzyme functionality.  We have developed a novel amino acid dehydrogenase (AADH) with broad substrate specificity.

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.  Constraint of mutant library size was guided by mechanistic and structural knowledge, ultimately reducing the screening requirements while maintaining an increased chance of generating alternate substrate specificity.

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See more of this Session: Advances In Biocatalysis and Biosynthesis II
See more of this Group/Topical: Food, Pharmaceutical & Bioengineering Division