| IED ID | IndEnz0010001041 |
| Enzyme Type ID | esterase001041 |
| Protein Name |
Monoacylglycerol lipase MAG lipase EC 3.1.1.23 |
| Gene Name | MGL2 YMR210W YM8261.04 |
| 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 | MRLKELLPNFLIVHQEVPEDPIAFKSTDKRENENKEITIPELIDTKVPELADGATDTLYGLLVNGHLQTAYGSFRHFDNIYKVQYKRMIIKYPHGGEGTVDFAVNGRSTKRRKVEKEYVPTSQPVFNGNLKRRYSYYSPDDPKLNSDDAKPMLIILHGLTGGSRESYVRAIVHEITTKYDFEACVFNARGCCYSAITTPLLYNGGWTNDIRYCVNDLRKRFPNRKFYMMGFSLGASIMTNYLGEESDRTKIECAISVSNPFDLYNSAYFINSTPMGSRFYSPALGHNLLRMVRNHLSTLEENPDFKDVIEKHLKKIRTVRQFDNLLTGPMFGYKNAEEYYKNASSYKRIPGIRTPFIALHAQDDPIVGGDLPIDQIKSNPYTLLLETSTGGHVGWFKDRSGRRWYAEPLCRFLKIFHDEITVKGLKPDLENVQLPDPNCEPIATTFRAN |
| Enzyme Length | 449 |
| Uniprot Accession Number | Q03649 |
| Absorption | |
| Active Site | ACT_SITE 232; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P28321; ACT_SITE 364; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P28321; ACT_SITE 392; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P28321 |
| 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:26991558}; 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:26991558};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960; Evidence={ECO:0000305|PubMed:26991558}; CATALYTIC ACTIVITY: Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629, ChEBI:CHEBI:75555; Evidence={ECO:0000269|PubMed:26991558};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38364; Evidence={ECO:0000305|PubMed:26991558}; 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:26991558};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000305|PubMed:26991558}; |
| DNA Binding | |
| EC Number | 3.1.1.23 |
| Enzyme Function | FUNCTION: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a preference for palmitoyl-MAG (PubMed:26991558). Does not play a significant role in ethyl ester biosynthesis (PubMed:16361250). Also possesses ester hydrolase and low but persistent TAG lipase activity (PubMed:29225428). {ECO:0000269|PubMed:16361250, ECO:0000269|PubMed:26991558, ECO:0000269|PubMed:29225428}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius for MAG lipase activity (PubMed:26991558). Optimum temperature is 45 degrees Celsius for p-nitrophenyl palmitate and 30 degrees Celsius for both p-nitrophenyl acetate and p-nitrophenyl butyrate (PubMed:29225428). {ECO:0000269|PubMed:26991558, ECO:0000269|PubMed:29225428}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for MAG lipase activity. Active over a broad pH range from pH 6 to pH 9 (PubMed:26991558). Optimum pH is 8.5 for p-nitrophenyl palmitate and pH 7.5 for both p-nitrophenyl acetate and p-nitrophenyl butyrate (PubMed:29225428). {ECO:0000269|PubMed:26991558, ECO:0000269|PubMed:29225428}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Cross-link (1); Domain (1); Motif (1); Mutagenesis (1) |
| Keywords | Hydrolase;Isopeptide bond;Reference proteome;Serine esterase;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10688190; 14690591; 15699485; 18719252; 19536198; 21255318; 22940803; |
| Motif | MOTIF 230..234; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:P28321 |
| Gene Encoded By | |
| Mass | 51,438 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.89 uM for palmitoyl-MAG {ECO:0000269|PubMed:26991558}; KM=11.51 uM for p-nitrophenyl acetate {ECO:0000269|PubMed:29225428}; KM=7.28 uM for p-nitrophenyl butyrate {ECO:0000269|PubMed:29225428}; KM=13.19 uM for p-nitrophenyl palmitate {ECO:0000269|PubMed:29225428}; Vmax=36.76 nmol/min/mg enzyme for MAG lipase activity {ECO:0000269|PubMed:26991558}; Vmax=0.26 umol/min/mg enzyme towards p-nitrophenyl butyrate {ECO:0000269|PubMed:26991558}; Vmax=0.18 umol/min/mg enzyme towards p-nitrophenyl acetate {ECO:0000269|PubMed:26991558}; Vmax=0.33 umol/min/mg enzyme towards p-nitrophenyl palmitate {ECO:0000269|PubMed:26991558}; |
| Metal Binding | |
| Rhea ID | RHEA:39959; RHEA:39960; RHEA:38363; RHEA:38364; RHEA:38487; RHEA:38488 |
| Cross Reference Brenda |