WARF TECHNOLOGIES

UW-Madison researchers have developed a highly efficient biocatalytic route for production of diverse γ-hydroxy amino acids starting from L-aspartate and readily available aldehydes. The method leverages an engineered variant of the enzyme UstD, which is natively involved in the biosynthesis of Ustiloxin D. Through protein engineering/directed evolution, the researchers identified a series of mutations that increased the catalytic activity of UstD, thereby improving its potential utility as a biocatalyst. The mutant UstD enzyme is compatible with virtually any hydrocarbon aldehyde substrate as well as a subset of hydrocarbon ketones, yielding a variety of γ-hydroxy amino acids, the vast majority of which show the formation of only a single diastereomer. These range from sterically demanding aryl aldehydes (biphenyl-4-carboxaldehyde) to electronically deactivated aryl aldehydes (4-hydroxybenzaldehyde) to aliphatic aldehydes (glycolaldehyde).

For More Information About the Inventors

• Andrew Buller

Tech Fields

• Drug Discovery & Development : Drug production & design