Biology:Lysophospholipase

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lysophospholipase
Identifiers
EC number3.1.1.5
CAS number9001-85-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Lysophospholipase, catalytic region
Identifiers
SymbolPLA2_B
PfamPF01735
InterProIPR002642
SMARTSM00022
PROSITEPDOC51210

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

2-lysophosphatidylcholine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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 InterProIPR000008. 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

  • Charcot-Leyden crystals

References

  1. "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca2+-dependent lipid-binding domain and a Ca2+-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. 1994. doi:10.1016/S0021-9258(17)32440-7. PMID 8027085. 
  2. 2.0 2.1 "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. 1994. doi:10.1016/S0021-9258(17)32081-1. PMID 8051052. 

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR002642