Interactions of thiophosphatidic acid with enzymes which metabolize phosphatidic acid. Inhibition of phosphatidic acid phosphatase and utilization by CDP-diacylglycerol synthase

Modelling lipid metabolism in plants: a slippery problem?

“…Mindful of these conflicting results, we carried out careful experiments with different concentrations of bromo-octanoate or bromo-palmitate in order to determine if specific inhibition of diacylglycerol acyltransferase could be obtained. For phosphatidate phosphohydrolase, such inhibitors have been reported [19], and may prove of utility in testing whether this enzyme is as important in plants as it is in controlling TAG synthesis in animals [20]. At concentrations of 0.02-0.03 mM, we obtained 15-20% inhibition of the enzyme routinely, without any significant alteration in total lipid labelling.…”

Phosphatidic Acid Mediates the Nem1-Spo7/Pah1 Phosphatase Cascade in Yeast Lipid Synthesis

“…For example, thioPA, the phosphorothioate analog of PA, did not stimulate Nem1-Spo7 activity. Parenthetically, thioPA is not a substrate for the PAP reaction ( 100 ). Additionally, DAG lacking the phosphate moiety of a phospholipid molecule did not stimulate the protein phosphatase activity.…”

“…ThioPA (C18:1) was synthesized as described by Bonnel et al. ( 100 ) with some modifications. Details on the synthesis and characterization of this phospholipid are found in the Supporting information .…”