Detail Information for IndEnz0005000205
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