IED Industry Enzyme Database

Detail Information for IndEnz0005001403
IED ID IndEnz0005001403
Enzyme Type ID lipase001403
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
Gene Name ABHD4
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MADDLEQQSQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPEQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGSDTWIDTSTGKKVKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEEICDSVD
Enzyme Length 342
Uniprot Accession Number Q8TB40
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.-
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 Alternative sequence (2); Chain (1); Domain (1); Sequence conflict (1)
Keywords Alternative splicing;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome
Interact With Q9NWT8; Q12982; Q96DZ9-2; P29400-2; Q9BUN8; Q6ZPD8; Q9BUP3-3; P24593; Q9Y5U4; O60664; Q9UI14; Q00765
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16818490; 21900206; 22488300; 32868797;
Motif
Gene Encoded By
Mass 38,794
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