Phosphatidylserine-specific phospholipase A1 (PLA1A)

Phosphatidylserine-specific phospholipase A1 (PLA1A) is a secreted enzyme that hydrolyzes the sn-1 acyl bond of phosphatidylserine and 1-acyl-2-lysophosphatidylserine, thus generating fatty acids and lysophosphatidylserine[3][2]. PLA1A activity participates in the remodeling of membrane phospholipids and modulates signaling related to immune cell activation, especially in mast cells in the context of apoptosis[3]. The enzyme is a member of the pancreatic lipase gene family and is characterized by a Ser-His-Asp catalytic triad, with unique substrate specificity for phosphatidylserine and a preference for short “lid” and “beta9 loop” domains which guide ligand binding and selectivity[1][2]. Mutations or dysregulation of PLA1A may contribute to inflammatory pathways and genetic syndromes involving lipid metabolism[3]. No specific approved drugs directly targeting PLA1A are currently known.

Other names

Phospholipase A1 member APLA1ANMDPSPLA1PS-PLA1ps-PLA1phosphatidylserine-specific phospholipase A1phosphatidylserine-specific phospholipase A1alpha

Hydrolysis of the sn-1 acyl bond of phosphatidylserine and lysophosphatidylserine leading to production of lysophosphatidylserine and fatty acids