Acyl-protein thioesterase 2 (LYPLA2)

Acyl-protein thioesterase 2 (LYPLA2) is an enzyme with hydrolase activity that regulates membrane lipid composition and protein localization by hydrolyzing fatty acids from S-acylated cysteine residues of various proteins, such as certain G protein subunits, HRAS, and GAP43[1][2]. It also acts as a lysophospholipase, catalyzing the removal of acyl groups from lysophospholipids, and participates in the hydrolysis of prostaglandin glycerol esters, implicating it in lipid mediator metabolism and cell signaling[1][2][4]. LYPLA2 plays a crucial role in lipid homeostasis and cellular signaling, and its dysfunction is associated with several neurological and degenerative diseases[1][2][4]. Its paralog, LYPLA1, has overlapping but non-redundant functions.

Other names

Lysophospholipase IIAPT2LPL-IILysoPLA IIpalmitoyl-protein hydrolaseDJ886K2.4testicular tissue protein Li 3

Inhibitors prevent hydrolysis of fatty acyl moieties from proteins, altering protein localization and function. Modulation of lysophospholipid and prostaglandin metabolism, affecting lipid-mediated signaling pathways.