The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
| 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 | ||||||||
| |||||||||
| Lysophospholipase, catalytic region | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | PLA2_B | ||||||||||
| Pfam | PF01735 | ||||||||||
| InterPro | IPR002642 | ||||||||||
| SMART | SM00022 | ||||||||||
| PROSITE | PDOC51210 | ||||||||||
| |||||||||||
- 2-lysophosphatidylcholine + H2O 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
editHuman genes encoding proteins that contain this domain include:
See also
editReferences
edit- ^ 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.
- ^ 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
edit- 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.
