Lysophospholipase

lysophospholipase
Identifiers
EC no.3.1.1.5
CAS no.9001-85-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Lysophospholipase, catalytic region
Identifiers
SymbolPLA2_B
PfamPF01735
InterProIPR002642
SMARTSM00022
PROSITEPDOC51210
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDBPDB: 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:

See also

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. ^ 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. 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". Methods Enzymol. 71 Pt. C: 513–21. doi:10.1016/0076-6879(81)71061-9. 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
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3.1.1: Carboxylic
ester hydrolases3.1.2: Thioesterase3.1.3: Phosphatase3.1.4:
Phosphodiesterase3.1.6: SulfataseNuclease (includes
deoxyribonuclease
and ribonuclease)
3.1.11-16:
Exonuclease
Exodeoxyribonuclease
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    
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