Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6

Definition:

Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-1-phosphate.

References:

[1]. Sumitra Miriyala, et al. Functional characterization of the atypical integral membrane lipid phosphatase PDP1/PPAPDC2 identifies a pathway for interconversion of isoprenols and isoprenoid phosphates in mammalian cells. J Biol Chem. 2010 Apr 30;285(18):13918-29. [Content Brief]

[2]. Koichi Fukunaga, et al. Identification and functional characterization of a presqualene diphosphate phosphatase. J Biol Chem. 2006 Apr 7;281(14):9490-7. [Content Brief]

[3]. Troy Carlo, et al. Activation of polyisoprenyl diphosphate phosphatase 1 remodels cellular presqualene diphosphate. Biochemistry. 2009 Apr 7;48(13):2997-3004. [Content Brief]

[4]. Troy Carlo, et al. 15-Epi-lipoxin A4 inhibits human neutrophil superoxide anion generation by regulating polyisoprenyl diphosphate phosphatase 1. FASEB J. 2013 Jul;27(7):2733-41. [Content Brief]

[5]. Spyros Theofilopoulos, et al. Novel function of the human presqualene diphosphate phosphatase as a type II phosphatidate phosphatase in phosphatidylcholine and triacylglyceride biosynthesis pathways. Biochim Biophys Acta. 2008 Nov-Dec;1781(11-12):731-42. [Content Brief]

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