IED ID | IndEnz0005000912 |
Enzyme Type ID | lipase000912 |
Protein Name |
Lipid droplet-associated triacylglycerol lipase TAG lipase EC 3.1.1.3 |
Gene Name | YPR147C |
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 | MTVKEYTKSKLPCSILNIKPTVTKSGEDAPLLVWIPGNPGLLYYYQEMLHHLHLKHPDWEILGISHAGMTLNAHSNTPIFSLQDQVDHQVEVINNFSCKNRKIIIMGHSVGAYIVQKVCLSNKLVGSVQKVGLVTPTVMDIHTSEMGIKMTAALRYIPPLAHVVSLFSYIFFYWILSEGFSRFIIDKFMGCGSTGYQAVLSTRIFLTHRQFVRQSLGLAAQEMEEITTNWEFQDRFINYCEENGISIWFLFSSNDHWVSGKTRSHLSDYYKDKVKQERLKIDVTDKIPHSFVVKHAEYAINAFF |
Enzyme Length | 304 |
Uniprot Accession Number | Q06522 |
Absorption | |
Active Site | ACT_SITE 109; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
Activity Regulation | |
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:29491250}; |
DNA Binding | |
EC Number | 3.1.1.3 |
Enzyme Function | FUNCTION: Shows both triacylglycerol (TAG) lipase and ester hydrolase activities. May play a role in TAG homeostasis. {ECO:0000269|PubMed:29491250}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30X degrees Celsius. {ECO:0000269|PubMed:29491250}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:29491250}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Glycosylation (1); Intramembrane (1); Motif (1); Topological domain (2) |
Keywords | Glycoprotein;Hydrolase;Lipid droplet;Membrane;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24868093}. Membrane {ECO:0000255}; Peripheral membrane protein {ECO:0000255}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 14562095; 16606443; 16884526; 17351896; 19536198; 21541367; |
Motif | MOTIF 107..111; /note=GXSXG; /evidence=ECO:0000255 |
Gene Encoded By | |
Mass | 34,842 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.07 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:29491250}; KM=14.79 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:29491250}; Note=kcat is 0.87 sec(-1) with p-nitrophenyl acetat as substrate and 0.44 sec(-1) with p-nitrophenyl butyrate as substrate. {ECO:0000269|PubMed:29491250}; |
Metal Binding | |
Rhea ID | RHEA:12044 |
Cross Reference Brenda |