Lysophospholipase
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The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
- 2-lysophosphatidylcholine + H2O 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.[1] Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids,[2] the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.[2]
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:
See also
References
Further reading
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