Phospholipid phosphatase 6 (PLPP6)

Phospholipid phosphatase 6 (PLPP6) is a magnesium-independent enzyme that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl, and geranylgeranyl diphosphates. It functions predominantly in the innate immune response by dephosphorylating presqualene diphosphate, a potent inhibitor of polymorphonuclear neutrophil activation pathways. PLPP6 is involved in cholesterol and sterol biosynthesis, as well as in the regulation of protein prenylation through its activity on farnesyl and geranylgeranyl diphosphates. While it exhibits lower activity toward phosphatidic acid, it may also participate in the biosynthesis of phospholipids and triacylglycerols, and can act on substrates such as ceramide-1-phosphate, lysophosphatidic acid, and sphingosine-1-phosphate[1][2][6]. Note: There is no evidence of approved interacting drugs or clinical biomarkers directly associated with PLPP6 to date. It is considered a potential therapeutic target based on its enzymatic role in lipid metabolism and immune regulation[2][1].

Other names

PDP1Presqualene diphosphate phosphatasePPAPDC2Phosphatidic acid phosphatase type 2 domain-containing protein 2Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6Phosphatidic acid phosphatase type 2 domain containing 2Polyisoprenoid diphosphate phosphatase type 1Type 1 polyisoprenoid diphosphate phosphataseLipid phosphatase-related protein-BPA-PSP

Inhibition or modulation of phosphatase activity affecting cholesterol biosynthesis and immune signaling