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

2-lysophosphatidylcholine + H₂O glycerophosphocholine + a carboxylate

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 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.^[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:

PLA2G4A, PLA2G4B, PLA2G4C, PLA2G4D, PLA2G4E, PLA2G4F

References

^ Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.
^ ^a ^b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052.

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Lysophospholipase, catalytic region
Identifiers
Symbol	PLA2_B
Pfam	PF01735
InterPro	IPR002642
SMART	SM00022
PROSITE	PDOC51210
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

lysophospholipase
Identifiers
EC number	3.1.1.5
CAS number	9001-85-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

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英: lysophospholipase

-lysophospholipase

[PUB00002859-1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.

[PUB00002865-2] Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052.

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lysophospholipase