IED ID | IndEnz0005000205 |
Enzyme Type ID | lipase000205 |
Protein Name |
Lyso -N-acylphosphatidylethanolamine lipase EC 3.1.1.- Alpha/beta hydrolase domain-containing protein 4 Abhydrolase domain-containing protein 4 Alpha/beta-hydrolase 4 Protein ABHD4 EC 3.-.-.- |
Gene Name | ABHD4 |
Organism | Bos taurus (Bovine) |
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
Enzyme Sequence | MADDLEQQPQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPELRDRTPLVMVHGFGGGVGLWILNMDSLSTRRTLHTFDLLGFGRSSRPTFPRDPEGAEDEFVTSIETWRESMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPADPSQVRAPPTWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFDDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGANTWIDTSTGKKVKLQRPDSYVRDLEIEGASHHVYADQPHIFNAVVEEICDSVD |
Enzyme Length | 342 |
Uniprot Accession Number | Q5EA59 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N,1-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:62537, ChEBI:CHEBI:85216; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45461; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:85217, ChEBI:CHEBI:85226; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45385; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-octadecanoyl-sn-glycero-3-phospho-ethanolamine; Xref=Rhea:RHEA:45388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:85219, ChEBI:CHEBI:85227; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45389; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N-eicosanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-eicosanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:85221, ChEBI:CHEBI:85228; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45393; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:85222, ChEBI:CHEBI:85229; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45397; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:85223, ChEBI:CHEBI:85230; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45401; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-2-hydroxy-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H(+); Xref=Rhea:RHEA:55236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:138661, ChEBI:CHEBI:138662; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55237; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = (9Z)-octadecenoate + 1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H(+); Xref=Rhea:RHEA:55240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:137009, ChEBI:CHEBI:138663; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55241; Evidence={ECO:0000250|UniProtKB:Q8VD66}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a fatty acid + H(+) + N-acyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:85216, ChEBI:CHEBI:85225; Evidence={ECO:0000250|UniProtKB:Q8VD66};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45421; Evidence={ECO:0000250|UniProtKB:Q8VD66}; |
DNA Binding | |
EC Number | 3.1.1.-; 3.-.-.- |
Enzyme Function | FUNCTION: Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine. {ECO:0000250|UniProtKB:Q8VD66}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (1) |
Keywords | Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,797 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:45424; RHEA:45425; RHEA:45460; RHEA:45461; RHEA:45384; RHEA:45385; RHEA:45388; RHEA:45389; RHEA:45392; RHEA:45393; RHEA:45396; RHEA:45397; RHEA:45400; RHEA:45401; RHEA:55236; RHEA:55237; RHEA:55240; RHEA:55241; RHEA:45420; RHEA:45421 |
Cross Reference Brenda |