6CHJ

Wax ester synthase/diacylglycerol acyltransferase from Marinobacter aquaeolei VT8

Summary for 6CHJ

• Entry DOI: 10.2210/pdb6chj/pdb
• Descriptor: Diacylglycerol O-acyltransferase, CHLORIDE ION (3 entities in total)
• Functional Keywords: ws/dgat, wax ester synthase, diacylglycerol acyltransferase, transferase
• Biological source: Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
• Total number of polymer chains: 2
• Total formula weight: 103290.54

Authors

Petronikolou, N.,Satish, S.K. (deposition date: 2018-02-22, release date: 2018-06-13, Last modification date: 2024-04-03)

Primary citation

Petronikolou, N.,Nair, S.K.
Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.
Acs Catalysis, 8:6334-6344, 2018

PubMed Abstract: 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.

PubMed: 31559109
DOI: 10.1021/acscatal.8b00787

Experimental method

X-RAY DIFFRACTION (2.428 Å)