| IED ID | IndEnz0005000023 |
| Enzyme Type ID | lipase000023 |
| Protein Name |
Monoglyceride lipase MGL EC 3.1.1.23 Fatty acid ethyl ester hydrolase FAEE hydrolase Monoacylglycerol hydrolase MAG hydrolase MGH Monoacylglycerol lipase MAG lipase MAGL Serine hydrolase YJU3 |
| Gene Name | YJU3 YKL094W YKL441 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MAPYPYKVQTTVPELQYENFDGAKFGYMFWPVQNGTNEVRGRVLLIHGFGEYTKIQFRLMDHLSLNGYESFTFDQRGAGVTSPGRSKGVTDEYHVFNDLEHFVEKNLSECKAKGIPLFMWGHSMGGGICLNYACQGKHKNEISGYIGSGPLIILHPHTMYNKPTQIIAPLLAKFLPRVRIDTGLDLKGITSDKAYRAFLGSDPMSVPLYGSFRQIHDFMQRGAKLYKNENNYIQKNFAKDKPVIIMHGQDDTINDPKGSEKFIQDCPSADKELKLYPGARHSIFSLETDKVFNTVFNDMKQWLDKHTTTEAKP |
| Enzyme Length | 313 |
| Uniprot Accession Number | P28321 |
| Absorption | |
| Active Site | ACT_SITE 123; /note=Nucleophile; /evidence=ECO:0000305|PubMed:26869448; ACT_SITE 251; /note=Charge relay system; /evidence=ECO:0000305|PubMed:26869448; ACT_SITE 281; /note=Charge relay system; /evidence=ECO:0000305|PubMed:26869448 |
| 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:20554061}; CATALYTIC ACTIVITY: Reaction=a fatty acid ethyl ester + H2O = a fatty acid + ethanol + H(+); Xref=Rhea:RHEA:50148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:28868, ChEBI:CHEBI:78206; Evidence={ECO:0000269|PubMed:27036938}; 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:20554061, ECO:0000269|PubMed:26869448};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000305|PubMed:20554061}; 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:20554061};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000305|PubMed:20554061}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:27036938};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960; Evidence={ECO:0000305|PubMed:20554061, ECO:0000305|PubMed:27036938}; 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:20554061};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; Evidence={ECO:0000305|PubMed:20554061}; CATALYTIC ACTIVITY: Reaction=ethyl hexadecanoate + H2O = ethanol + H(+) + hexadecanoate; Xref=Rhea:RHEA:50132, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:84932; Evidence={ECO:0000269|PubMed:27036938};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50133; Evidence={ECO:0000305|PubMed:27036938}; CATALYTIC ACTIVITY: Reaction=ethyl (9Z)-octadecenoate + H2O = (9Z)-octadecenoate + ethanol + H(+); Xref=Rhea:RHEA:50136, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:30823, ChEBI:CHEBI:84940; Evidence={ECO:0000269|PubMed:27036938};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50137; Evidence={ECO:0000305|PubMed:27036938}; CATALYTIC ACTIVITY: Reaction=ethyl (9Z)-hexadecenoate + H2O = (9Z)-hexadecenoate + ethanol + H(+); Xref=Rhea:RHEA:50144, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:32372, ChEBI:CHEBI:84934; Evidence={ECO:0000269|PubMed:27036938};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50145; Evidence={ECO:0000305|PubMed:27036938}; CATALYTIC ACTIVITY: Reaction=ethyl octadecanoate + H2O = ethanol + H(+) + octadecanoate; Xref=Rhea:RHEA:50316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:25629, ChEBI:CHEBI:84936; Evidence={ECO:0000269|PubMed:27036938};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50317; Evidence={ECO:0000305|PubMed:27036938}; |
| DNA Binding | |
| EC Number | 3.1.1.23 |
| Enzyme Function | FUNCTION: Converts monoacylglycerides (MAG) to free fatty acids and glycerol (PubMed:20554061). Has a strong preference for monounsaturated monoglycerides (PubMed:26869448). Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA) (PubMed:19529773). Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-oxidative metabolites of ethanol that are transiently incorporated into lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases facilitates a controlled metabolism of these potentially toxic lipid metabolites (PubMed:27036938). {ECO:0000269|PubMed:19529773, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:26869448, ECO:0000269|PubMed:27036938}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active from pH 4.5 to 8. {ECO:0000269|PubMed:20554061}; |
| Pathway | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000269|PubMed:20554061}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (11); Chain (1); Helix (14); Motif (1); Sequence conflict (2); Turn (5) |
| Keywords | 3D-structure;Cytoplasm;Endoplasmic reticulum;Hydrolase;Lipid droplet;Membrane;Mitochondrion;Mitochondrion outer membrane;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Cytoplasm {ECO:0000269|PubMed:11914276}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}. Note=Although the protein is identified in the cytoplasm, several membrane systems and lipid droplets, MGL activity is only measured in membrane fractions and lipid droplets. {ECO:0000269|PubMed:20554061}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4ZWN; 4ZXF; |
| Mapped Pubmed ID | 10998572; 14690591; 16434153; 16606443; 18467557; 19536198; 20056167; 20231294; 22345606; 22970195; 23275493; 24678285; 25894691; 26991558; |
| Motif | MOTIF 121..125; /note=GXSXG; /evidence=ECO:0000305|Ref.14 |
| Gene Encoded By | |
| Mass | 35,563 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=260 uM for rac-1(3)-oleoylglycerol {ECO:0000269|PubMed:20554061}; Vmax=10.3 mmol/h/mg enzyme {ECO:0000269|PubMed:20554061}; |
| Metal Binding | |
| Rhea ID | RHEA:50148; RHEA:38487; RHEA:38488; RHEA:38491; RHEA:38492; RHEA:39959; RHEA:39960; RHEA:39963; RHEA:39964; RHEA:50132; RHEA:50133; RHEA:50136; RHEA:50137; RHEA:50144; RHEA:50145; RHEA:50316; RHEA:50317 |
| Cross Reference Brenda |