| IED ID | IndEnz0005000341 |
| Enzyme Type ID | lipase000341 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Extracellular lipase Lactonizing lipase Lipase P Triacylglycerol ester hydrolase |
| Gene Name | lipL |
| Organism | Pseudomonas sp. (strain 109) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Proteobacteria incertae sedis unclassified pseudomonads Pseudomonas sp. (strain 109) |
| Enzyme Sequence | MKKKSLLPLGLAIGLASLAASPLIQASTYTQTKYPIVLAHGMLGFDNILGVDYWFGIPSALRRDGAQVYVTEVSQLDTSEVRGEQLLQQVEEIVALSGQPKVNLIGHSHGGPTIRYVAAVRPDLMPSATSVGAPHKGSDTADFLRQIPPGSAGEAVLSGLVNSLGALISFLSSGSAGTQNSLGSLESLNSEGAARFNAKYPQGIPTSACGEGAYKVNGVSYYSWSGSSPLTNFLDPSDAFLGASSLTFKNGTANDGLVGTCSSHLGMVIRDNYRMNHLDEVNQVFGLTSLFETSPVSVYRQHANRLKNASL |
| Enzyme Length | 311 |
| Uniprot Accession Number | P26877 |
| Absorption | |
| Active Site | ACT_SITE 108; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P26876; ACT_SITE 255; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26876; ACT_SITE 277; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26876 |
| Activity Regulation | |
| Binding Site | BINDING 42; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P26876; BINDING 109; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P26876 |
| 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:0000305|PubMed:1917947}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. Also able to catalyze, in anhydrous organic solvents, intramolecular transesterification of omega-hydroxyfatty acid esters to form macrocyclic lactones. This biosynthesis is dependent on the chain length of the substrates, and the formation of monomer lactone is maximum with methyl 18-hydroxyoctadecanoate. With shorter substrates, monomer lactone decreases and the formation of diolide (dimer lactone) increases. {ECO:0000269|PubMed:1917947}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Disulfide bond (1); Domain (1); Metal binding (4); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26876}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:1917947 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,737 |
| Kinetics | |
| Metal Binding | METAL 235; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P26876; METAL 279; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P26876; METAL 283; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P26876; METAL 287; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P26876 |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |