- Examples
- References
- Further reading
| Name = lysophospholipase
| EC_number = 3.1.1.5
| CAS_number = 9001-85-8
| IUBMB_EC_number = 3/1/1/5
| GO_code = 0004622
| image =
| width =
| caption =
}}{{Pfam box |Symbol = PLA2_B |Name = Lysophospholipase, catalytic region |Pfam = PF01735 |InterPro = IPR002642 |SMART = SM00022 |PROSITE = PDOC51210 |PDB = {{PDB|1cjy}} }}
In enzymology, a lysophospholipase ({{EC number|3.1.1.5}}) is an enzyme that catalyzes the chemical reaction
2-lysophosphatidylcholine + H2Oglycerophosphocholine + 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 number|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
References
2. ^1 {{cite journal |vauthors=Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE |title=The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity |journal=J. Biol. Chem. |volume=269 |issue=31 |pages=19725–19730 |year=1994 |pmid=8051052}}
Further reading
{{refbegin}}- {{cite journal | vauthors = Abe M, Ohno K, Sato R | last-author-amp = yes | year = 1974 | title = Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction | journal = Biochim. Biophys. Acta | volume = 369 | pages = 361–370 | doi = 10.1016/0005-2760(74)90150-7 }}
- {{cite journal | vauthors = Contardi A, Ercoli A | last-author-amp = yes | year = 1933 | title = The enzymic cleavage of lecithin and lysolecithin | journal = Biochem. Z. | volume = 261 | pages = 275–302 }}
- {{cite journal | author = Dawson RMC | year = 1958 | title = Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation | journal = Biochem. J. | volume = 70 | pages = 559–570 }}
- {{cite journal | author = Fairbairn D | year = 1948 | title = The preparation and properties of a lysophospholipase from Penicillium notatum | journal = J. Biol. Chem. | volume = 173 | pages = 705–714 }}
- {{cite journal | author = SHAPIRO B | year = 1953 | title = Purification and properties of a lysolecithinase from pancreas | journal = Biochem. J. | volume = 53 | pages = 663–6 | pmid = 13032127 | issue = 4 | pmc = 1198209 }}
- {{cite journal | vauthors = van den Bosch H, Aarsman AJ, de Jong JG, van Deenem LL | year = 1973 | title = Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas | journal = Biochim. Biophys. Acta | volume = 296 | pages = 94–104 | pmid = 4693514 | issue = 1 | doi = 10.1016/0005-2760(73)90048-9 }}
- {{cite journal | vauthors = van den Bosch H, Vianen GM, van Heusden GP | year = 1981 | title = Lysophospholipase--transacylase from rat lung | journal = Methods Enzymol. 71 Pt | volume = C | pages = 513–21 | pmid = 7278668 | doi=10.1016/0076-6879(81)71061-9}}
- {{cite journal | vauthors = van Tienhoven M, Atkins J, Li Y, Glynn P | year = 2002 | title = Human neuropathy target esterase catalyzes hydrolysis of membrane lipids | journal = J. Biol. Chem. | volume = 277 | pages = 20942–8 | pmid = 11927584 | doi = 10.1074/jbc.M200330200 | issue = 23 }}
- {{cite journal | vauthors = Quistad GB, Barlow C, Winrow CJ, Sparks SE, Casida JE | year = 2003 | title = Evidence that mouse brain neuropathy target esterase is a lysophospholipase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | pages = 7983–7 | pmid = 12805562 | doi = 10.1073/pnas.1232473100 | issue = 13 | pmc = 164699 }}
- {{cite journal | vauthors = Lush MJ, Li Y, Read DJ, Willis AC, Glynn P | date = 1998 | title = Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man | journal = Biochem. J. | volume = 332 | pages = 1–4 | pmid = 9576844 | pmc = 1219444 | issue = Pt 1 }}
- {{cite journal | vauthors = Winrow CJ, Hemming ML, Allen DM, Quistad GB, Casida JE, Barlow C | year = 2003 | title = Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity | journal = Nat. Genet. | volume = 33 | pages = 477–85 | pmid = 12640454 | doi = 10.1038/ng1131 | issue = 4 }}
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