The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B (EC 3.1.1.5) and cytosolic phospholipase A<sub>2</sub> which also has a C2 domain . Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells. Cytosolic phospholipase A<sub>2</sub> associates with natural membranes in response to physiological increases in Ca<sup>2+</sup> and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the carboxy-terminal Ca<sup>2+</sup>-independent catalytic domain of the protein as discussed in.
The systematic name of this enzyme class is 2-lysophosphatidylcholine acylhydrolase. Other names in common use include lecithinase B, lysolecithinase, phospholipase B, lysophosphatidase, lecitholipase, phosphatidase B, lysophosphatidylcholine hydrolase, lysophospholipase A1, lysophopholipase L2, lysophospholipase transacylase, neuropathy target esterase, NTE, NTE-LysoPLA, and NTE-lysophospholipase. This enzyme participates in glycerophospholipid metabolism.
Human genes encoding proteins that contain this domain include: