Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) Have Different Specificities in Their Forward and Reverse Reactions

Authors

• Ida Lager, Swedish University of Agricultural SciencesFollow
• Jenny Lindberg Yilmaz, Biotechnology Research AB
• Xue-Rong Zhou, CSIRO Food & Nutrition, Sydney, AustraliaFollow
• Katarzyna Jasieniecka, University of Gdansk and Medical University of Gdansk
• Michael Kazachkov, National Research Council of Canada, Saskatoon
• Peng Wang, University of Nebraska-LincolnFollow
• Jitao Zou, eNational Research Council of Canada, Saskatoon
• Randall Weselake, University of Alberta, Edmonton
• Mark A. Smith, eNational Research Council of Canada, SaskatoonFollow
• Shen Bayon, State University, Pullman
• John M. Dyer, United States Department of Agriculture-Agricultural Research Service, Maricopa
• Jay Shockey, USDA-ARS, New OrleansFollow
• Ernst Heinz, University of Hamburg
• Allan Green, Commonwealth Scientific and Industrial Research Organisation Plant Industry
• Antoni Banas, University of Gdansk and Medical University of Gdansk
• Sten Stymne, Swedish University of Agricultural Sciences

Document Type

Article

Date of this Version

2014

Citation

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 288, NO. 52, pp. 36902–36914, December 27, 2013

Comments

Published in the U.S.A.

Abstract

Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine.

Results: Plant LPCATs were expressed in yeast and biochemically characterized.

Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions.

Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid.