| IED ID | IndEnz0005001177 |
| Enzyme Type ID | lipase001177 |
| Protein Name |
Lipid droplet phospholipase 1 EC 3.1.-.- EC 3.1.1.4 |
| Gene Name | LPL1 YOR059C YOR29-10 |
| 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 | MTSDKHLFVLIHGLWGNYTHMESMRTILSTTLKKEDVNDDMIYFLPKQNAMFKTFDGIEIIGYRTLIEVCEFIRDYKDGKITKLSVMGYSQGGLVARFMIGKMLTEFKELFEDIEPQLFITMATPHLGVEFYNPTGIAYKSALYSALRTLGSTILGKSGREMFIANSSNNILVKLSQGEYLEALSLFKWRIAFANVKNDRTVAFYTAFITDCDPFIDFDNKLKYTFEEKIPGSGYKGILPKIVDLNALNVNSHAPTKPTKTYKKWGRTILIILVATFLILPIALVMNGLGTAYSYIVTCKYRKMLSNGILHNEVRGKLGLTEQLKGYVTDAYGSIINSALDMDANYEASNSNLVNEEELPWKEFIQKYTTINDGVWKSKFKKLPFDENRKVILRNLNKLKWIRVPIYIKAVNAHGVIVARRGMDENTAATGIACIEFTAQLLAYLMHKSN |
| Enzyme Length | 450 |
| Uniprot Accession Number | Q08448 |
| Absorption | |
| Active Site | ACT_SITE 90; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + H2O = a fatty acid + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:32967, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32968; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycero-3-phosphate + a fatty acid + H(+); Xref=Rhea:RHEA:44420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57970, ChEBI:CHEBI:58608; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44421; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 1-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+); Xref=Rhea:RHEA:44672, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:64379; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44673; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoglycerol + H2O = a 2-acyl-sn-glycero-3-phosphoglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:62032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:145393, ChEBI:CHEBI:145394; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62033; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:62036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:28868, ChEBI:CHEBI:78421; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62037; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphoglycerol + H2O = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:62044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:145392, ChEBI:CHEBI:145393; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62045; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=an N-aryl-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = an N-aryl-1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62048, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:145395, ChEBI:CHEBI:145396; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62049; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + a fatty acid + H(+); Xref=Rhea:RHEA:62052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:74544, ChEBI:CHEBI:145397; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62053; Evidence={ECO:0000269|PubMed:25014274}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62100, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:73005; Evidence={ECO:0000269|PubMed:25014274};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62101; Evidence={ECO:0000269|PubMed:25014274}; |
| DNA Binding | |
| EC Number | 3.1.-.-; 3.1.1.4 |
| Enzyme Function | FUNCTION: Phospholipase involved in maintaining the lipid droplet morphology (PubMed:25014274). Has phospholipase activity with broad substrate specificity, acting on glycerophospholipids phosphatidylethanolamine (PE), phosphatidic acid (PA), phosphatidycholine (PC) and phosphatidylserine (PS), primarily at sn-2 position (PubMed:25014274). It can later remove fatty acids from the sn-1 position of the produced lysophospholipids such as lysophosphatidylethanolamine (LPE) (PubMed:25014274). Shows also activity toward phosphatidylglycerol, but, in contrast to what was observed with the other phospholipids tested, prefers the sn-1 position (PubMed:25014274). {ECO:0000269|PubMed:25014274}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Motif (1); Mutagenesis (3); Transmembrane (1) |
| Keywords | Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Expression is up-regulated by the transcription factor RPN4. {ECO:0000269|PubMed:19073890}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:25014274}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10998572; 11283351; 11805826; 16429126; 19111628; 22842922; 23275493; 24040173; 24868093; 28928489; |
| Motif | MOTIF 88..92; /note=Lipase-specific GXSXG motif; /evidence=ECO:0000269|PubMed:25014274 |
| Gene Encoded By | |
| Mass | 51,106 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.86 mM for phosphatidylethanolamine (PE) {ECO:0000269|PubMed:25014274}; KM=0.97 mM for phosphatidic acid (PA) {ECO:0000269|PubMed:25014274}; KM=1.12 mM for phosphatidylglycerol (PG) {ECO:0000269|PubMed:25014274}; KM=0.83 mM for phosphatidycholine (PC) {ECO:0000269|PubMed:25014274}; KM=0.92 mM for phosphatidylserine (PS) {ECO:0000269|PubMed:25014274}; Vmax=4.55 umol/min/mg enzyme toward phosphatidylethanolamine (PE) {ECO:0000269|PubMed:25014274}; Vmax=4.05 umol/min/mg enzyme toward phosphatidic acid (PA) {ECO:0000269|PubMed:25014274}; Vmax=3.25 umol/min/mg enzyme toward phosphatidylglycerol (PG) {ECO:0000269|PubMed:25014274}; Vmax=1.65 umol/min/mg enzyme toward phosphatidycholine (PC) {ECO:0000269|PubMed:25014274}; Vmax=1.05 umol/min/mg enzyme toward phosphatidylserine (PS) {ECO:0000269|PubMed:25014274}; |
| Metal Binding | |
| Rhea ID | RHEA:44604; RHEA:44605; RHEA:32967; RHEA:32968; RHEA:44420; RHEA:44421; RHEA:15801; RHEA:15802; RHEA:44672; RHEA:44673; RHEA:62032; RHEA:62033; RHEA:62036; RHEA:62037; RHEA:62044; RHEA:62045; RHEA:62048; RHEA:62049; RHEA:62052; RHEA:62053; RHEA:62100; RHEA:62101 |
| Cross Reference Brenda |