Improving asymmetric reductions by building reductase chimeras and the investigation of systematic reductase mutations

BIOL 212

Brent D. Feske, feskebre@mail.armstrong.edu1, Scott C. Mateer2, Crystal Archer3, Eric Davis3, and Ruchita Patel3. (1) Department of Chemistry and Physics, Armstrong Atlantic State University, 11935 Abercorn St, Savannah, GA 31419, (2) Department of Biology, Armstrong Atlantic State University, 11935 abercorn st, savannah, GA 31419, (3) Armstrong Atlantic State University, 11935 Abercorn St., savannah, GA 31419
Baker's yeast has been utilized by organic chemists as a biocatalytic tool to synthesize asymmetric alcohols. Recently, a set of 20 identified yeast reductases where fused to the GST epitope tag and cloned into E. coli to generate a GST-reductase library. This heterologous system has been used to characterize the stereoselectivity of each reductase for any given substrate. Once the stereoselectivity for a specific substrate-enzyme pair was established, the reductase was then systematically mutated in order to investigate the affects of these mutations on the enzyme's stereoselectivity.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007