Protein engineering for development of new hydrolytic biocatalysts

• Published in: Current Opinion in Chemical Biology
• Main Author: Widersten, Mikael
• Format: Article in Journal/Newspaper
• Language: English
• Published: Uppsala universitet, Institutionen för kemi - BMC 2014
• Subjects: Biochemistry and Molecular Biology; Biokemi och molekylärbiologi; Antarc*; Antarctica
• Online Access: http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-221378; https://doi.org/10.1016/j.cbpa.2014.03.015

Hydrolytic enzymes play important roles as biocatalysts in chemical synthesis. The chemical versatility and structurally sturdy features of Candida antarctica lipase B has placed this enzyme as a common utensil in the synthetic tool-box. In addition to catalyzing acyl transfer reactions, a number of promiscuous activities have been described recently. Some of these new enzyme activities have been amplified by mutagenesis. Epoxide hydrolases are of interest due to their potential as catalysts in asymmetric synthesis. This current update discusses recent development in the engineering of lipases and epoxide hydrolases aiming to generate new biocatalysts with refined features as compared to the wild-type enzymes. Reported progress in improvements in reaction atom economy from dynamic kinetic resolution or enantioconvergence are also included.