Summary: Lysophospholipase catalytic domain
This is the Wikipedia entry entitled "Lysophospholipase". More...
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Lysophospholipase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
|Lysophospholipase, catalytic region|
- 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 220.127.116.11 and cytosolic phospholipase A2 which also has a C2 domain 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. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, 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.
Human genes encoding proteins that contain this domain include:
- 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 Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.
- 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. PMID 8051052.
- 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 (4): 663–6. 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. PMID 4693514.
- van den Bosch H, Vianen GM, van Heusden GP (1981). "Lysophospholipase--transacylase from rat lung". Methods Enzymol. 71 Pt C: 513–21. doi:10.1016/0076-6879(81)71061-9. 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. doi:10.1073/pnas.1232473100. PMC 164699. 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 (Pt 1): 1–4. 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.
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Lysophospholipase catalytic domain Provide feedback
This family consists of Lysophospholipase / phospholipase B EC:18.104.22.168 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain PF00168. Phospholipase B enzymes catalyse the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells . Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids  the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in .
Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD; , J Biol Chem 1994;269:18239-18249.: Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain. PUBMED:8027085 EPMC:8027085
Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE; , J Biol Chem 1994;269:19725-19730.: The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity. PUBMED:8051052 EPMC:8051052
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002642This family consists of lysophospholipase / phospholipase B EC and cytosolic phospholipase A2 which also has a C2 domain INTERPRO. Phospholipase B enzymes catalyse the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells [PUBMED:8027085]. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids [PUBMED:8051052], the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in [PUBMED:8051052].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||phospholipase activity (GO:0004620)|
|Biological process||phospholipid catabolic process (GO:0009395)|
- the number of sequences which exhibit this architecture
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Curation and family details
|Seed source:||Pfam-B_2127 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||15|
|Number in full:||966|
|Average length of the domain:||338.50 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||56.67 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PLA2_B domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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