title: Identification of a residue affecting fatty alcohol selectivity in wax ester synthase.
abstract: The terminal enzyme in the bacterial wax ester biosynthetic pathway is the bifunctional wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase (WS/DGAT), which utilizes a fatty alcohol and a fatty acyl-coenzyme A (CoA) to synthesize the corresponding wax ester. In this report, we identify a specific residue in WS/DGAT enzymes obtained from Marinobacter aquaeolei VT8 and Acinetobacter baylyi that alters fatty alcohol selectivity and kinetic parameters when modified to alternative residues.
authors.affiliation: Department of Bioproducts and Biosystems Engineering and BioTechnology Institute, University of Minnesota, St. Paul, Minnesota, USA. bbarney@umn.edu
authors.forename: Brett M
authors.initials: BM
authors.lastname: Barney
authors.forename: Rachel L
authors.initials: RL
authors.lastname: Mann
authors.forename: Janet M
authors.initials: JM
authors.lastname: Ohlert
mesh_terms: D000150:Acinetobacter / Q000201:enzymology* / Q000235:genetics; D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism*; D019943:Amino Acid Substitution; D005233:Fatty Alcohols / Q000378:metabolism*; D007700:Kinetics; D053520:Marinobacter / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity
chemical_list: D005233:Fatty Alcohols; D000217:Acyltransferases; C079165:long-chain-alcohol O-fatty-acyltransferase