Structural exploration of a novel enzymatic hydration mechanism

The enantioselective hydration of electron-rich C=C bonds is a synthetic challenge, particularly for the sustainable production of fine chemicals. Biocatalytic alternatives are developing, yet current options face limitations to their industrial application.

The enzyme Linalool Dehydratase-Isomerase (LDIase) enantioselectively adds water to myrcene in this way using a novel mechanism, further complemented by dehydration and isomerisation functions. This may not only bear a prospective biocatalytic tool for enantioselective hydration, but could also facilitate the manufacture of polymers from natural feedstocks.

To enable the application of LDIase as an industrial biocatalyst, this work further explored this enzyme’s mechanistic details using structural studies. A 2.58 Å resolution structure of an LDIase mutant was obtained which gave an initial indicator of a covalent intermediate. An aerobic homologue was also investigated as a possible industrial alternative.

A comprehensive understanding of this enzymatic hydration mechanism will allow rational engineering of LDIase to expand its substrate range, for the diverse production of highly valuable chemicals. By this method, we may reduce our reliance on non-renewable petrochemical sources and energy-intensive synthesis to produce natural chemicals of higher quality.