Lysophospholipase

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

2-lysophosphatidylcholine + H₂O $\rightleftharpoons$ glycerophosphocholine + a 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 Template:InterPro. 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.

Examples

Human genes encoding proteins that contain this domain include:

• PLA2G4A, PLA2G4B, PLA2G4C, PLA2G4D, PLA2G4E, PLA2G4F

See also

• Charcot-Leyden crystals

Further reading

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