title: Substrate specificity of diacylglycerol kinase-epsilon and the phosphatidylinositol cycle.
abstract: We show that diacylglycerol kinase-ε (DGKε) has less preference for the acyl chain at the sn-1 position of diacylglycerol (DAG) than the one at the sn-2 position. Although DGKε discriminates between 1-stearoyl-2-arachidonoyl-DAG and 1-palmitoyl-2-arachidonoyl-DAG, it has similar substrate preference for 1-stearoyl-2-arachidonoyl-DAG and 1,2-diarachidonoyl-DAG. We suggest that in addition to binding to the enzyme, the acyl chain at the sn-1 position may contribute to the depth of insertion of the DAG into the membrane. Thus, the DAG intermediate of the PI-cycle, 1-stearoyl-2-arachidonoyl-DAG, is not the only DAG that is a good substrate for DGKε, the DGK isoform involved in PI-cycling.
authors: Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
authors: Yulia V
authors: YV
authors: Shulga
authors: Matthew K
authors: MK
authors: Topham
authors: Richard M
authors: RM
authors: Epand
mesh_terms: D019852:Diacylglycerol Kinase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004075:Diglycerides / Q000737:chemistry / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D010716:Phosphatidylinositols / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D004075:Diglycerides; D004791:Enzyme Inhibitors; D010716:Phosphatidylinositols; C037149:stearoylarachidonylglycerol; C526464:DGKE protein, human; D019852:Diacylglycerol Kinase