IED Industry Enzyme Database

Detail Information for IndEnz0005001348
IED ID IndEnz0005001348
Enzyme Type ID lipase001348
Protein Name Monoacylglycerol lipase abhd6-A
EC 3.1.1.23
Abhydrolase domain-containing protein 6-A
Gene Name abhd6-a
Organism Xenopus laevis (African clawed frog)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog)
Enzyme Sequence MDLDVLNMFLVAGGTLLVPILAFVTSFLLWPAALIKIYYWYWRRALGMQVKFSSYGNYKFCYTSRGKPGNKASVLMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSALDDYSICGQVKRIHQFVESIGLNKRTFHLVGTSMGGNVAGVYAAQHPTDISSLTLICPAGLMYPTESKFLKHLKGLEKSGDDQRILLIPSTAGEMEDMLRLCSFVRFKIPQQVLQGLVDVRIPHNEFYRQLFMALVNEKSRHSLQENMNKIVAPTQIIWGKQDQVLDVSGAEVLAGSIRGCQVEILENCGHSVVMERPRKSAKLMTDFLSSLQSTENNKKHE
Enzyme Length 337
Uniprot Accession Number Q6GLL2
Absorption
Active Site ACT_SITE 148; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q99685; 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:0000250|UniProtKB:Q9BV23}; 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:0000250|UniProtKB:Q9BV23}; 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=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: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:0000250|UniProtKB:Q9BV23}; 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 (By similarity). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. 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. 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 (By similarity). {ECO:0000250|UniProtKB:Q8R2Y0, ECO:0000250|UniProtKB:Q9BV23}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Topological domain (2); Transmembrane (1)
Keywords Endosome;Hydrolase;Lipid metabolism;Lysosome;Membrane;Mitochondrion;Signal-anchor;Transmembrane;Transmembrane helix
Interact With
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
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 37,883
Kinetics
Metal Binding
Rhea ID RHEA:44328; RHEA:44320; RHEA:44316; RHEA:44312; RHEA:39963; RHEA:38491; RHEA:38487; RHEA:44732; RHEA:26132; RHEA:44728; RHEA:48428; RHEA:55712; RHEA:55716; RHEA:55804
Cross Reference Brenda