Structural highlights
Publication Abstract from PubMed
Wax esters are high-value products whose enzymatic synthesis is of increasing biotechnological interest. The fabrication of cell factories that mass-produce wax esters may provide a facile route towards a sustainable, and environment-friendly approach to a large-scale process for this commodity chemical. An expedient route for wax-ester biocatalysis may be facilitated by the action of enzymes termed wax ester synthases/diacylglycerol acyltransferases (WS/DGAT), which produce wax esters using fatty acids and alcohols as a precursor. In this work, we report the structure for a member of the WS/DGAT superfamily. The structural data in conjunction with bioinformatics and mutational analyses allowed us to identify the substrate binding pockets, and residues that may be important for catalysis. Using this information as a guide, we generated a mutant with preference towards shorter acyl-substrates. This study demonstrates the efficacy of a structure-guided engineering effort towards a WS/DGAT variant with preference towards wax esters of desired lengths.
Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.,Petronikolou N, Nair SK ACS Catal. 2018 Jul 6;8(7):6334-6344. doi: 10.1021/acscatal.8b00787. Epub 2018, Jun 1. PMID:31559109[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Petronikolou N, Nair SK. Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters. ACS Catal. 2018 Jul 6;8(7):6334-6344. doi: 10.1021/acscatal.8b00787. Epub 2018, Jun 1. PMID:31559109 doi:http://dx.doi.org/10.1021/acscatal.8b00787
