lysophospholipase

{{infobox enzyme

| Name = lysophospholipase

| EC_number = 3.1.1.5

| CAS_number = 9001-85-8

| 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}} }}

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 {{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.{{cite journal |vauthors=Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD |title=Delineation of two functionally distinct domains of cytosolic phospholipase A₂, a regulatory Ca²⁺-dependent lipid-binding domain and a Ca²⁺-independent catalytic domain |journal=J. Biol. Chem. |volume=269 |issue=27 |pages=18239–18249 |year=1994 |doi=10.1016/S0021-9258(17)32440-7 |pmid=8027085|doi-access=free }} Cytosolic phospholipase A₂ associates with natural membranes in response to physiological increases in Ca²⁺ and selectively hydrolyses arachidonyl phospholipids,{{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 |doi=10.1016/S0021-9258(17)32081-1 |pmid=8051052|doi-access=free }} 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

References

{{cite journal | vauthors = Abe M, Ohno K, Sato R | 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 | issue = 3 | pages = 361–370 | doi = 10.1016/0005-2760(74)90150-7 }}
{{cite journal | vauthors = Contardi A, Ercoli A | 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 | issue = 4 | pages = 559–570 | doi = 10.1042/bj0700559 | pmid = 13607409 | pmc = 1196709 }}
{{cite journal | author = Fairbairn D | year = 1948 | title = The preparation and properties of a lysophospholipase from Penicillium notatum | journal = J. Biol. Chem. | volume = 173 | issue = 2 | pages = 705–714 | doi = 10.1016/S0021-9258(18)57441-X | pmid = 18910725 | doi-access = free }}
{{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 | doi = 10.1042/bj0530663 | 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 book | vauthors = van den Bosch H, Vianen GM, van Heusden GP | chapter = Lysophospholipase—transacylase from rat lung| year = 1981 | title = Lipids Part C| series = Methods in Enzymology | volume = 71| pages = 513–21 | pmid = 7278668 | doi=10.1016/0076-6879(81)71061-9| isbn = 978-0-12-181971-2 }}
{{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 | doi-access = free }}
{{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 | bibcode = 2003PNAS..100.7983Q | doi-access = free }}
{{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 | doi = 10.1042/bj3320001 }}
{{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 | doi-access = free }}

Category:EC 3.1.1

Category:Enzymes of known structure

lysophospholipase

Examples

See also

References

Further reading