IED Industry Enzyme Database

Detail Information for IndEnz0005001353
IED ID IndEnz0005001353
Enzyme Type ID lipase001353
Protein Name Monoacylglycerol lipase ABHD6
EC 3.1.1.23
2-arachidonoylglycerol hydrolase
Abhydrolase domain-containing protein 6
Gene Name ABHD6
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 MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASVHNTDNNKKLD
Enzyme Length 337
Uniprot Accession Number Q9BV23
Absorption
Active Site ACT_SITE 148; /note="Nucleophile"; /evidence="ECO:0000250|UniProtKB:Q99685, ECO:0000305|PubMed:22969151"; ACT_SITE 278; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q99685"; ACT_SITE 306; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q99685"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-octanoylglycerol + H2O = glycerol + H(+) + octanoate; Xref=Rhea:RHEA:44328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:85241; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44329; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+); Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44321; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+); Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, ChEBI:CHEBI:75562; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75457; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75568; Evidence={ECO:0000269|PubMed:22969151};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429; Evidence={ECO:0000269|PubMed:22969151}; CATALYTIC ACTIVITY: Reaction=(S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:55712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152; Evidence={ECO:0000269|PubMed:26491015};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55713; Evidence={ECO:0000269|PubMed:26491015}; CATALYTIC ACTIVITY: Reaction=(S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:55716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:139156, ChEBI:CHEBI:139157; Evidence={ECO:0000250|UniProtKB:Q8R2Y0}; CATALYTIC ACTIVITY: Reaction=(R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+); Xref=Rhea:RHEA:55804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:139228, ChEBI:CHEBI:139230; Evidence={ECO:0000250|UniProtKB:Q8R2Y0};
DNA Binding
EC Number 3.1.1.23
Enzyme Function FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015). {ECO:0000250|UniProtKB:Q8R2Y0, ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:26491015}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-9 with 2-arachidonoyglycerol as substrate. {ECO:0000269|PubMed:22969151};
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Mutagenesis (1); Natural variant (5); Sequence conflict (2); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Endosome;Hydrolase;Lipid metabolism;Lysosome;Membrane;Mitochondrion;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix
Interact With Q9Y3D6; Q5QGT7; Q969E2; Q9NYZ1
Induction
Subcellular Location SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 7OTS;
Mapped Pubmed ID 18360779; 19793082; 21418147; 21988832; 22827915; 24534757; 26496610; 27114538; 28880480; 30728209; 30894461; 32143183;
Motif
Gene Encoded By
Mass 38,331
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=159 uM for 2-arachidonoyglycerol {ECO:0000269|PubMed:22969151}; Vmax=45 nmol/min/mg enzyme toward 2-arachidonoyglycerol {ECO:0000269|PubMed:22969151};
Metal Binding
Rhea ID RHEA:44328; RHEA:44329; RHEA:44320; RHEA:44321; RHEA:44316; RHEA:44312; RHEA:44313; RHEA:39963; RHEA:39964; RHEA:38491; RHEA:38492; RHEA:38487; RHEA:38488; RHEA:44732; RHEA:44733; RHEA:26132; RHEA:26133; RHEA:44728; RHEA:44729; RHEA:48428; RHEA:48429; RHEA:55712; RHEA:55713; RHEA:55716; RHEA:55804
Cross Reference Brenda