Mammalian Mg2+-independent Phosphatidate Phosphatase (PAP2) Displays Diacylglycerol Pyrophosphate Phosphatase Activity*

@article{Dillon1997MammalianMP,
  title={Mammalian Mg2+-independent Phosphatidate Phosphatase (PAP2) Displays Diacylglycerol Pyrophosphate Phosphatase Activity*},
  author={D. Dillon and X. Chen and G. M. Zeimetz and W. Wu and D. Waggoner and J. Dewald and D. Brindley and G. Carman},
  journal={The Journal of Biological Chemistry},
  year={1997},
  volume={272},
  pages={10361 - 10366}
}
Recent studies indicate that the metabolism of diacylglycerol pyrophosphate (DGPP) is involved in a novel lipid signaling pathway. DGPP phosphatases (DGPP phosphohydrolase) fromSaccharomyces cerevisiae and Escherichia colicatalyze the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyze the dephosphorylation of PA to yield diacylglycerol. We demonstrated that the Mg2+-independent form of PA phosphatase (PA phosphohydrolase, PAP2) purified from rat liver catalyzed the… Expand
Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae.
Phosphatidate phosphatase, a key regulator of lipid homeostasis.
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