| IED ID | IndEnz0010000527 |
| Enzyme Type ID | esterase000527 |
| Protein Name |
60 kDa lysophospholipase EC 3.1.1.5 Lysophospholipase-transacylase Includes: L-asparaginase EC 3.5.1.1 L-asparagine amidohydrolase ; 1-alkyl-2-acetylglycerophosphocholine esterase EC 3.1.1.47 Platelet-activating factor acetylhydrolase PAF acetylhydrolase |
| Gene Name | Aspg |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MARAMGPERRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLKTLHMFHDEEYAQAHSLPEDTLVLPPASPDQRIIYTVLECQPLFDSSDMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQPGLSLNDRKKLLAKDLRGEMTLPATDVLLQDGMLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSFKDSVCAQPQPH |
| Enzyme Length | 564 |
| Uniprot Accession Number | A0JNU3 |
| Absorption | |
| Active Site | ACT_SITE 19; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10100 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21017; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40879, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + octadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40887, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:25629, ChEBI:CHEBI:73858; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = H(+) + hexadecanoate + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40892; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40899, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998, ChEBI:CHEBI:73004, ChEBI:CHEBI:73005; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395, ChEBI:CHEBI:76079; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40903, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:76078; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40904; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=2 2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40907, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40908; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-O-(9Z)-octadecenoyl-2-O-acetyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-acetyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78044, ChEBI:CHEBI:78045; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41321; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) = a 1-acyl-2-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:41352, ChEBI:CHEBI:16870, ChEBI:CHEBI:64771, ChEBI:CHEBI:64874, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41353; Evidence={ECO:0000250|UniProtKB:O88202}; CATALYTIC ACTIVITY: Reaction=2 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40959, ChEBI:CHEBI:16870, ChEBI:CHEBI:60657, ChEBI:CHEBI:76079; Evidence={ECO:0000250|UniProtKB:O88202};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40960; Evidence={ECO:0000250|UniProtKB:O88202}; |
| DNA Binding | |
| EC Number | 3.1.1.5; 3.5.1.1; 3.1.1.47 |
| Enzyme Function | FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities (By similarity). Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer) (By similarity). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid (By similarity). {ECO:0000250|UniProtKB:O88202}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Modified residue (1); Region (3); Repeat (5) |
| Keywords | ANK repeat;Acyltransferase;Hydrolase;Lipid degradation;Lipid metabolism;Phosphoprotein;Reference proteome;Repeat;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 478; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 21267068; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,595 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177; RHEA:15178; RHEA:21016; RHEA:21017; RHEA:17777; RHEA:17778; RHEA:40435; RHEA:40436; RHEA:40879; RHEA:40880; RHEA:40887; RHEA:40888; RHEA:40807; RHEA:40808; RHEA:40891; RHEA:40892; RHEA:40895; RHEA:40896; RHEA:40899; RHEA:40900; RHEA:40827; RHEA:40828; RHEA:40903; RHEA:40904; RHEA:40907; RHEA:40908; RHEA:41320; RHEA:41321; RHEA:41352; RHEA:41353; RHEA:40959; RHEA:40960 |
| Cross Reference Brenda | 3.1.1.47; |