| IED ID | IndEnz0005000154 |
| Enzyme Type ID | lipase000154 |
| Protein Name |
Lipase 2 EC 3.1.1.3 Triacylglycerol lipase |
| Gene Name | lip2 L2 |
| Organism | Moraxella sp. (strain TA144) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Moraxella unclassified Moraxella Moraxella sp. (strain TA144) |
| Enzyme Sequence | MPILPVPALNALLTKTIKTIKTGAAKNAHQHHVLHHTLKGLDNLPAPVLERINRRLKASTAEQYPLADAHLRLILAISNKLKRPLAIDKLPKLRQKFGTDAVSLQAPSVWQQNADASGSTENAVSWQDKTIANADGGDMTVRCYQKSTQNSERKSTDEAAMLFFHGGGFCIGDIDTHHEFCHTVCAQTGWAVVSVDYRMAPEYPAPTALKDCLAAYAWLAEHSQSLGASPSRIVLSGDSAGGCLAALVAQQVIKPIDALWQDNNQAPAADKKVNDTFKNSLADLPRPLAQLPLYPVTDYEAEYPSWELYGEGLLLDHNDAEVFNSAYTQHSGLPQSHPLISVMHGDNTQLCPSYIVVAELDILRDEGLAYAELLQKEGVQVQTYTVLGAPHGFINLMSVHQGLGNQTTYIINEFACLVQNLLTSEGDKPNLRA |
| Enzyme Length | 433 |
| Uniprot Accession Number | P24484 |
| Absorption | |
| Active Site | ACT_SITE 239; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P23872, ECO:0000255|PROSITE-ProRule:PRU10038"; ACT_SITE 361; /evidence="ECO:0000250|UniProtKB:P23872"; ACT_SITE 391; /evidence="ECO:0000250|UniProtKB:P23872" |
| 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; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active at temperatures close to 0 degree Celsius.; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Motif (1); Mutagenesis (2) |
| Keywords | Hydrolase;Lipid degradation;Lipid metabolism |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 165..167; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
| Gene Encoded By | |
| Mass | 47,225 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |