Lysophospholipase Explained

lysophospholipase
Ec Number:	3.1.1.5
Cas Number:	9001-85-8
Go Code:	0004622

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

2-lysophosphatidylcholine + H₂O

\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 . 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.

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

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 . 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 . 10.1042/bj0700559 . 13607409 . 1196709 .
• Fairbairn D . 1948 . The preparation and properties of a lysophospholipase from Penicillium notatum . J. Biol. Chem. . 173 . 2 . 705 - 714 . 10.1016/S0021-9258(18)57441-X . 18910725 . free .
• SHAPIRO B . 1953 . Purification and properties of a lysolecithinase from pancreas . Biochem. J. . 53 . 663 - 6 . 13032127 . 4 . 10.1042/bj0530663 . 1198209 .
• 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 . 94 - 104 . 4693514 . 1 . 10.1016/0005-2760(73)90048-9 .
• Book: van den Bosch H, Vianen GM, van Heusden GP . Lysophospholipase—transacylase from rat lung. 1981 . Lipids Part C. Methods in Enzymology . 71. 513 - 21 . 7278668 . 10.1016/0076-6879(81)71061-9. 978-0-12-181971-2 .
• van Tienhoven M, Atkins J, Li Y, Glynn P . 2002 . Human neuropathy target esterase catalyzes hydrolysis of membrane lipids . J. Biol. Chem. . 277 . 20942 - 8 . 11927584 . 10.1074/jbc.M200330200 . 23 . free .
• 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 . 7983 - 7 . 12805562 . 10.1073/pnas.1232473100 . 13 . 164699 . 2003PNAS..100.7983Q . free .
• 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 . 1 - 4 . 9576844 . 1219444 . Pt 1 . 10.1042/bj3320001 .
• 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 . 477 - 85 . 12640454 . 10.1038/ng1131 . 4 . free .

Notes and References

1. Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD . 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 . 10.1016/S0021-9258(17)32440-7 . 8027085. free .
2. Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE . The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity . J. Biol. Chem. . 269 . 31 . 19725–19730 . 1994 . 10.1016/S0021-9258(17)32081-1 . 8051052. free .