Lysophospholipase

lysophospholipase
Identifiers
EC no.	3.1.1.5
CAS no.	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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

Lysophospholipase, catalytic region
Identifiers
Symbol	PLA2_B
Pfam	PF01735
InterPro	IPR002642
SMART	SM00022
PROSITE	PDOC51210
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB PDB: 1cjy ​

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

2-lysophosphatidylcholine + H₂O ${\displaystyle \rightleftharpoons }$ 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 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. ^[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

See also

• Charcot-Leyden crystals

References

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 Ca²⁺-dependent lipid-binding domain and a Ca²⁺-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. doi: 10.1016/S0021-9258(17)32440-7 . PMID   8027085.
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. doi: 10.1016/S0021-9258(17)32081-1 . PMID   8051052.

Further reading

• Abe M, Ohno K, Sato R (1974). "Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction". Biochim. Biophys. Acta. 369 (3): 361–370. doi:10.1016/0005-2760(74)90150-7.
• Contardi A, Ercoli A (1933). "The enzymic cleavage of lecithin and lysolecithin". Biochem. Z. 261: 275–302.
• Dawson RMC (1958). "Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation". Biochem. J. 70 (4): 559–570. doi:10.1042/bj0700559. PMC   1196709 . PMID   13607409.
• Fairbairn D (1948). "The preparation and properties of a lysophospholipase from Penicillium notatum". J. Biol. Chem. 173 (2): 705–714. doi: 10.1016/S0021-9258(18)57441-X . PMID   18910725.
• SHAPIRO B (1953). "Purification and properties of a lysolecithinase from pancreas". Biochem. J. 53 (4): 663–6. doi:10.1042/bj0530663. PMC   1198209 . PMID   13032127.
• van den Bosch H, Aarsman AJ, de Jong JG, van Deenem LL (1973). "Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas". Biochim. Biophys. Acta. 296 (1): 94–104. doi:10.1016/0005-2760(73)90048-9. PMID   4693514.
• van den Bosch H, Vianen GM, van Heusden GP (1981). "Lysophospholipase—transacylase from rat lung". Lipids Part C. Methods in Enzymology. Vol. 71. pp. 513–21. doi:10.1016/0076-6879(81)71061-9. ISBN   978-0-12-181971-2. PMID   7278668.
• van Tienhoven M, Atkins J, Li Y, Glynn P (2002). "Human neuropathy target esterase catalyzes hydrolysis of membrane lipids". J. Biol. Chem. 277 (23): 20942–8. doi: 10.1074/jbc.M200330200 . PMID   11927584.
• Quistad GB, Barlow C, Winrow CJ, Sparks SE, Casida JE (2003). "Evidence that mouse brain neuropathy target esterase is a lysophospholipase". Proc. Natl. Acad. Sci. U.S.A. 100 (13): 7983–7. Bibcode:2003PNAS..100.7983Q. doi: 10.1073/pnas.1232473100 . PMC   164699 . PMID   12805562.
• Lush MJ, Li Y, Read DJ, Willis AC, Glynn P (1998). "Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man". Biochem. J. 332 (Pt 1): 1–4. doi:10.1042/bj3320001. PMC   1219444 . PMID   9576844.
• Winrow CJ, Hemming ML, Allen DM, Quistad GB, Casida JE, Barlow C (2003). "Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity". Nat. Genet. 33 (4): 477–85. doi: 10.1038/ng1131 . PMID   12640454.

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