Identification of a Residue Affecting Fatty Alcohol Selectivity in Wax Ester Synthase | Zendy

Brett M. Barney | Zendy; Rachel L. Mann | Zendy; Janet M. Ohlert | Zendy

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Identification of a Residue Affecting Fatty Alcohol Selectivity in Wax Ester Synthase

Author(s) -

Brett M. Barney,

Rachel L. Mann,

Janet M. Ohlert

Publication year - 2012

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.02523-12

Subject(s) - wax ester , fatty alcohol , wax , biochemistry , residue (chemistry) , enzyme , coenzyme a , chemistry , alcohol , phosphofructokinase 2 , fatty acid , reductase

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 fromMarinobacter aquaeolei VT8 andAcinetobacter baylyi that alters fatty alcohol selectivity and kinetic parameters when modified to alternative residues.

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