Lysophospholipase

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In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction

2-lysophosphatidylcholine + H₂O glycerophosphocholine + 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. 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.

Contents 1 Structural studies 2 References 3 External links 3.1 Gene Ontology (GO) codes

Structural studies

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1G86, 1HDK, 1IVN, 1J00, 1JRL, 1LCL, 1QKQ, 1U8U, 1V2G, 2G07, 2G08, 2G09, and 2G0A.

References

• IUBMB entry for 3.1.1.5
• BRENDA references for 3.1.1.5 (Recommended.)
• PubMed references for 3.1.1.5
• PubMed Central references for 3.1.1.5
• Google Scholar references for 3.1.1.5
• Abe M, Ohno K and Sato R (1974). "Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction". Biochim. Biophys. Acta 369: 361–370.
• Contardi A and 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: 559–570.
• Fairbairn D (1948). "The preparation and properties of a lysophospholipase from Penicillium notatum". J. Biol. Chem. 173: 705–714.
• SHAPIRO B (1953). "Purification and properties of a lysolecithinase from pancreas". Biochem. J. 53: 663–6. 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: 94–104. PMID 4693514.
• van den Bosch H, Vianen GM, van Heusden GP (1981). "Lysophospholipase--transacylase from rat lung". Methods. Enzymol. 71 Pt C: 513–21. 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: 20942–8. 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: 7983–7. PMID 12805562.
• Lush MJ, Li Y, Read DJ, Willis AC, Glynn P (Pt 1). "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. 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: 477–85. PMID 12640454.

External links

The CAS registry number for this enzyme class is 9001-85-8.

• IUBMB entry for 3.1.1.5

• KEGG entry for 3.1.1.5

• BRENDA entry for 3.1.1.5

• NiceZyme view of 3.1.1.5

• EC2PDB: PDB structures for 3.1.1.5

• PRIAM entry for 3.1.1.5

• PUMA2 entry for 3.1.1.5

• IntEnz: Integrated Enzyme entry for 3.1.1.5

• MetaCyc entry for 3.1.1.5

• Atomic-resolution structures of enzymes belonging to this class

Gene Ontology (GO) codes

• EGO entry for GO code 0004622: lysophospholipase

• AMIGO entry for GO code 0004622: lysophospholipase