Lysophosphatidic acid phosphatase type 6 (ACP6)

Lysophosphatidic acid phosphatase type 6 (ACP6) is a member of the histidine acid phosphatase family that acts specifically on lysophosphatidic acid (LPA), hydrolyzing it to produce monoacylglycerol and phosphate[2][3][5]. This enzyme is highly active at acidic pH, displays preference for medium chain LPAs (notably myristate, palmitate, oleate), and regulates key steps of lipid metabolism, especially within mitochondria[2][5][6]. ACP6 is involved in modulating signaling pathways mediated by LPA through G protein-coupled receptors and helps maintain cellular lipid balance. Dysregulation of ACP6 expression can lead to abnormal LPA levels, promoting oncogenic processes such as increased cell proliferation, migration, and invasion in several cancers including ovarian and esophageal carcinoma, positioning ACP6 as a possible tumor suppressor[4][5]. The structure of ACP6 includes a conserved Rossmann-fold-like domain and a substrate pocket tailored for LPA, with catalytic activity relying on a cluster of key residues. Key findings indicate ACP6's clinical significance as a potential prognostic biomarker, although no drugs are currently known to target this enzyme directly.

Other names

Acid phosphatase 6, lysophosphatidicACPL1LPAPPACPL1Acid phosphatase-like protein 1

Enzymatic hydrolysis of LPA to reduce its accumulation, thus influencing LPA-mediated signaling pathways, particularly those involving G protein-coupled receptors[1][2][5].