Function
PLA2G4B is a calcium-dependent phospholipase A1 and A2, and lysophospholipase, potentially playing a role in membrane phospholipid remodeling. It functions as a calcium-dependent phospholipase A2 and lysophospholipase. PLA2G4B cleaves the ester bond of the fatty acyl group attached to the sn-2 position of phosphatidylethanolamines, producing lysophospholipids that may be involved in deacylation-reacylation cycles. While it hydrolyzes lysophosphatidylcholines with low efficiency, it is inefficient toward phosphatidylcholines.
Additionally, PLA2G4B acts as a calcium-dependent phospholipase A1 and A2, and lysophospholipase. It cleaves the ester bond of the fatty acyl group attached to the sn-1 or sn-2 position of diacyl phospholipids (phospholipase A1 and A2 activity, respectively), producing lysophospholipids that may be used in deacylation-reacylation cycles. PLA2G4B can further hydrolyze lysophospholipids, enabling complete deacylation. However, it exhibits no activity toward alkylacyl phospholipids.