Lysophospholipase

In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H₂O, whereas its two products are glycerophosphocholine and carboxylate.

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 A2 which also has a C2 domain InterPro: IPR000008. 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 A2 associates with natural membranes in response to physiological increases in Ca²⁺ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the carboxy-terminal Ca²⁺-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.