| IED ID | IndEnz0005000904 |
| Enzyme Type ID | lipase000904 |
| Protein Name |
Lipase, thermostable EC 3.1.1.3 Triacylglycerol lipase Fragment |
| Gene Name | |
| Organism | Burkholderia cepacia (Pseudomonas cepacia) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia Burkholderia cepacia complex Burkholderia cepacia (Pseudomonas cepacia) |
| Enzyme Sequence | AVDDYAATRYPIILVHGLTTDSKYGGVVEYXYRNPNDLTSHXXAAYVYELRSDPLD |
| Enzyme Length | 56 |
| Uniprot Accession Number | P29605 |
| Absorption | |
| Active Site | |
| 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 | FUNCTION: This thermostable and solvent-tolerant lipase is rather nonspecific. It can synthesize both primary and secondary alcohol esters. Simple triglycerides of short and middle chain fatty acids (C<13) are the preferred substrates. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable.; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;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 | |
| Gene Encoded By | |
| Mass | 6,314 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |