-!- This enzyme catalyzes the Mg(2+)-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. -!- In lipid signaling, the enzyme generates a pool of DAG to be used for protein kinase C activation. -!- The mammalian enzymes are known as lipins.

-!- The bifunctional enzyme catalyzes the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. EC 3.1.3.4). -!- It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signaling role in stress response. -!- The phosphatase activity of the bifunctional enzyme is Mg(2+)- independent and N-ethylmaleimide-insensitive and is distinct from the Mg(2+)-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4. -!- The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase.

-!- Isolated from the bacteria Micrococcus lysodeikticus, Escherichia coli and Bacillus subtilis. -!- The product of the reaction, ditrans,octacis-undecaprenyl phosphate, is essential for cell wall polysaccharide biosynthesis in these strains.