| IED ID | IndEnz0005000978 |
| Enzyme Type ID | lipase000978 |
| Protein Name |
Triacylglycerol lipase 3 EC 3.1.1.3 Lipase 3 |
| Gene Name | TGL3 YMR313C YM9924.05C |
| 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 | MKETAQEYKVSAVIPTLLKNWILRVVYATLDHIPPFVWEILHVITDIYFFWVQKLINYVRPHSRVIYYNAIKKLDECDTYQMWCQQASVVDEITGANLWRRNFFSRRYDFNSVIEQYSILENMLREEKYDVVKEKFSTTGPCMLRNFAGIGDKKLFTKSLMGTKLLIEQYLTRILEGLDILNNQTLTPTSFFQRCKLSLGTTALILQGGSLFGLFHLGVIRGLLLQDLMPNIISGSSMGACVASLFGCLSNEQLKQLLTDDNLLNIIKNDVDLLKSCGYGNLEQHLNLGTLIQNLIHHGYSQDVYLFIRFVMKYIVKEKTFEEVYQITGKVFNIVIHPTDKSCPNLLNYVTTPNVLIKSAIECSLGSGVISEDTSLLCKNLENEIEPFLNINKNKQVKFLTPENANNPSITESPYTRLTELFNVNNFIVSLARPYLAPLVVNDLKHEIKTSKYYYYKHYPNMPPINANTVRKTQRSSSQSPIKAGTVEDLEPEPLMSPVPPSSAVNDSAEYIIPELGIPQLNFTEMEPLAFKFKYHLERKLKNIATMEFRHRMEVLDNLGLLCSLIKRLIIDEKTPRSATEIAVVPRMKSLSLTRIIEGQLNNIPYWIKSGERSTWPALALIKTRCAVEFKLDDIIRARRSR |
| Enzyme Length | 642 |
| Uniprot Accession Number | P40308 |
| Absorption | |
| Active Site | ACT_SITE 237; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 403; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q12043 |
| Activity Regulation | ACTIVITY REGULATION: Loses its lipolytic activity in cells lacking nonpolar lipids. {ECO:0000269|PubMed:23673660}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:12682047};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:12682047}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:20016004};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:16267052, ECO:0000305|PubMed:20016004}; CATALYTIC ACTIVITY: Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:16267052};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869; Evidence={ECO:0000305|PubMed:16267052}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphoethanolamine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37731, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:64381, ChEBI:CHEBI:75238; Evidence={ECO:0000269|PubMed:20016004};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37732; Evidence={ECO:0000305|PubMed:20016004}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37767, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:64381, ChEBI:CHEBI:75265; Evidence={ECO:0000269|PubMed:20016004};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37768; Evidence={ECO:0000305|PubMed:20016004}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:10515935, PubMed:12682047, PubMed:16267052). Also catalyzes the acylation of lysophosphatidic acid (LPA). Important for efficient sporulation, but rather through its acyltransferase than lipase activity (PubMed:20016004). {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:12682047, ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:20016004}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Motif (2); Mutagenesis (1); Region (1); Sequence conflict (2) |
| Keywords | Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:12682047, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:23673660, ECO:0000269|PubMed:24868093}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols. {ECO:0000269|PubMed:23673660}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10998572; 11283351; 15218532; 16246075; 16916618; 16919863; 18258205; 18269180; 18367008; 19037676; 19150427; 19536198; 19696439; 19841731; 20056167; 20231294; 20452973; 20727985; 21060891; 22345606; 22989772; 23042128; 23139841; 23275493; 23631861; 24007978; 24373967; 24390141; 24418527; 24520995; 24597968; 24678285; 24847060; 25016085; 25461829; 25475986; 25500271; 25713391; 25894691; 26018144; 26061644; 26636650; 26907989; 27170177; 27230908; 27932491; |
| Motif | MOTIF 235..239; /note="GXSXG"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"; MOTIF 298..303; /note="HXXXXD acyltransferase motif"; /evidence="ECO:0000305|PubMed:20016004, ECO:0000305|Ref.10" |
| Gene Encoded By | |
| Mass | 73,613 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for 1-acyl-sn-glycero-3-phosphoethanolamine {ECO:0000269|PubMed:20016004}; KM=18 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20016004}; Vmax=46.26 nmol/min/mg enzyme towards 1-acyl-sn-glycero-3-phosphoethanolamine {ECO:0000269|PubMed:20016004}; Vmax=44.25 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20016004}; |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:12045; RHEA:38575; RHEA:38576; RHEA:47868; RHEA:47869; RHEA:37731; RHEA:37732; RHEA:37767; RHEA:37768 |
| Cross Reference Brenda |