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

作者: Deirdre A. Dillon , Xiaoming Chen , Geri Marie Zeimetz , Wen-I. Wu , David W. Waggoner

DOI: 10.1074/JBC.272.16.10361

关键词:

摘要: 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 dephosphorylation to yield phosphatidate (PA) then catalyze PA diacylglycerol. We demonstrated Mg2+-independent form phosphatase (PA phosphohydrolase, PAP2) purified from rat liver catalyzed DGPP. This reaction was Mg2+-independent, insensitive inhibition byN-ethylmaleimide bromoenol lactone, inhibited by Mn2+ ions. PAP2 exhibited high affinity for (Km = 0.04 mol %). The specificity constant (Vmax/Km) 1.3-fold higher than PA. ability dephosphorylate PA, Like PAP2, activity S. cerevisiaewas lyso-PA, sphingosine 1-phosphate, ceramide 1-phosphate. Mouse showed homology fromS. E. coli, especially localized regions constitute sequence motif. Collectively, our work indicated member family includes coli. propose model which activities regulate cellular levels DGPP,

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