| IED ID | IndEnz0005001404 |
| Enzyme Type ID | lipase001404 |
| Protein Name |
Monoacylglycerol lipase ABHD6 EC 3.1.1.23 2-arachidonoylglycerol hydrolase Abhydrolase domain-containing protein 6 |
| Gene Name | Abhd6 |
| 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 | MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYAHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIVGQVKRIHQFVECLKLNKKPFHLIGTSMGGHVAGVYAAYYPSDVCSLSLVCPAGLQYSTDNPFVQRLKELEESAAIQKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNSFYRKLFLEIVNEKSRYSLHENMDKIKVPTQIIWGKQDQVLDVSGADILAKSISNSQVEVLENCGHSVVMERPRKTAKLIVDFLASVHNTDNKKLN |
| Enzyme Length | 336 |
| Uniprot Accession Number | Q8R2Y0 |
| Absorption | |
| Active Site | ACT_SITE 148; /note=Nucleophile; /evidence=ECO:0000305|PubMed:24095738; 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:18096503, ECO:0000269|PubMed:24095738}; 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:18096503};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:18096503}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:26491015};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:26491015}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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:0000269|PubMed:26491015};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55717; Evidence={ECO:0000269|PubMed:26491015}; 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:0000269|PubMed:26491015};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55805; Evidence={ECO:0000269|PubMed:26491015}; |
| DNA Binding | |
| EC Number | 3.1.1.23 |
| Enzyme Function | FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:18096503, PubMed:20657592). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (PubMed:18096503, PubMed:20657592). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (PubMed:24095738). 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:0000269|PubMed:18096503, ECO:0000269|PubMed:20657592, ECO:0000269|PubMed:24095738, ECO:0000269|PubMed:26491015}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:26491015}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Erroneous initiation (2); Mutagenesis (1); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Endosome;Hydrolase;Lipid metabolism;Lysosome;Membrane;Mitochondrion;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Up-regulated in small intestine and liver by high-fat diet. {ECO:0000269|PubMed:24095738}. |
| Subcellular Location | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:26491015}; Single-pass type II membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:26491015}; Single-pass type II membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:20657592}; Single-pass type II membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 18799693; 21665953; 22632720; 23806692; 24101490; 24814481; 26494286; 26909310; 26997277; 27114538; 27783937; 29688375; 33201859; 33444462; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,205 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for 1(3)-monoolein {ECO:0000269|PubMed:24095738}; KM=0.75 uM for 1-oleoyl lysophosphatidylglycerol (in presence of 5M CHAPS) {ECO:0000269|PubMed:24095738}; KM=0.98 mM for (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) {ECO:0000269|PubMed:26491015}; KM=0.9 mM for racemic monoolein {ECO:0000269|PubMed:26491015}; KM=1.1 mM for lysophosphatidylglycerol {ECO:0000269|PubMed:26491015}; Vmax=478.6 umol/h/mg enzyme toward 1(3)-monoolein {ECO:0000269|PubMed:24095738}; Vmax=93.2 umol/h/mg enzyme toward 1-oleoyl lysophosphatidylglycerol {ECO:0000269|PubMed:24095738}; Vmax=89 umol/h/mg enzyme toward lysophosphatidylglycerol {ECO:0000269|PubMed:26491015}; Vmax=348 umol/h/mg enzyme toward (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol) {ECO:0000269|PubMed:26491015}; Vmax=806 umol/h/mg enzyme toward 1-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:26491015}; |
| Metal Binding | |
| Rhea ID | RHEA:26132; RHEA:26133; RHEA:44328; RHEA:44320; RHEA:44316; RHEA:44312; RHEA:39963; RHEA:38491; RHEA:38487; RHEA:38488; RHEA:44732; RHEA:44728; RHEA:48428; RHEA:55712; RHEA:55713; RHEA:55716; RHEA:55717; RHEA:55804; RHEA:55805 |
| Cross Reference Brenda |