| IED ID | IndEnz0005000983 |
| Enzyme Type ID | lipase000983 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Cold-adapted lipase Extracellular lipase Triacylglycerol ester hydrolase |
| Gene Name | lips SAMN05216594_0967 |
| Organism | Pseudomonas fragi |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas chlororaphis group Pseudomonas fragi |
| Enzyme Sequence | MDDSVNTRYPILLVHGLFGFDRIGSHHYFHGIKQALNECGASVFVPIISAANDNEARGDQLLKQIHNLRRQVGAQRVNLIGHSQGALTARYVAAIAPELIASVTSVSGPNHGSELADRLRLAFVPGRLGETVAAALTTSFSAFLSALSGHPRLPQNALNALNALTTDGVAAFNRQYPQGLPDRWGGMGPAQVNAVHYYSWSGIIKGSRLAESLNLLDPLHNALRVFDSFFTRETRENDGMVGRFSSHLGQVIRSDYPLDHLDTINHMARGSRRRINPVELYIEHAKRLKEAGL |
| Enzyme Length | 293 |
| Uniprot Accession Number | P08658 |
| Absorption | |
| Active Site | ACT_SITE 83; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P26876; ACT_SITE 238; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26876; ACT_SITE 260; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26876 |
| Activity Regulation | |
| Binding Site | BINDING 17; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P22088; BINDING 84; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P22088 |
| 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:12084074, ECO:0000269|PubMed:6052627, ECO:0000305|PubMed:15848176}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerols, with the highest activity with tributyrin (C4), lower activity with tricaprylin (C8), and much lower activity with triacetin (C2), trilaurin (C12) and triolein (C18). {ECO:0000269|PubMed:12084074, ECO:0000269|PubMed:15848176, ECO:0000269|PubMed:6052627}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 29 degrees Celsius (PubMed:12084074). Stable at 10 degrees Celsius, but above this temperature the activity decreases. The enzyme is completely inactivated at 40 degrees Celsius (PubMed:6052627, PubMed:12084074). {ECO:0000269|PubMed:12084074, ECO:0000269|PubMed:6052627}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.8-9. {ECO:0000269|PubMed:12084074, ECO:0000269|PubMed:6052627}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Domain (1); Frameshift (2); Metal binding (4); Mutagenesis (3) |
| Keywords | Calcium;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:3060375, ECO:0000305|PubMed:5881339}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,086 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 mM for tributyrin {ECO:0000269|PubMed:6052627}; |
| Metal Binding | METAL 217; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P26876; METAL 262; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P26876; METAL 266; /note=Calcium; /evidence=ECO:0000305|PubMed:12084074; METAL 269; /note=Calcium; /evidence=ECO:0000305|PubMed:12084074 |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda | 3.1.1.3; |