| IED ID | IndEnz0005000680 |
| Enzyme Type ID | lipase000680 |
| Protein Name |
Lipase EC 3.1.1.3 Lipase II RNL Triacylglycerol lipase |
| Gene Name | |
| Organism | Rhizopus niveus |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Mucoromycota Mucoromycotina Mucoromycetes Mucorales (pin molds) Mucorineae Rhizopodaceae Rhizopus Rhizopus niveus |
| Enzyme Sequence | MVSFISISQGVSLCLLVSSMMLGSSAVPVSGKSGSSNTAVSASDNAALPPLISSRCAPPSNKGSKSDLQAEPYNMQKNTEWYESHGGNLTSIGKRDDNLVGGMTLDLPSDAPPISLSSSTNSASDGGKVVAATTAQIQEFTKYAGIAATAYCRSVVPGNKWDCVQCQKWVPDGKIITTFTSLLSDTNGYVLRSDKQKTIYLVFRGTNSFRSAITDIVFNFSDYKPVKGAKVHAGFLSSYEQVVNDYFPVVQEQLTAHPTYKVIVTGHSLGGAQALLAGMDLYQREPRLSPKNLSIFTVGGPRVGNPTFAYYVESTGIPFQRTVHKRDIVPHVPPQSFGFLHPGVESWIKSGTSNVQICTSEIETKDCSNSIVPFTSILDHLSYFDINEGSCL |
| Enzyme Length | 392 |
| Uniprot Accession Number | P61871 |
| Absorption | |
| Active Site | ACT_SITE 268; /note=Nucleophile; /evidence=ECO:0000305|PubMed:8902613; ACT_SITE 327; /note=Charge relay system; /evidence=ECO:0000305|PubMed:8902613; ACT_SITE 380; /note=Charge relay system; /evidence=ECO:0000305|PubMed:8902613 |
| Activity Regulation | ACTIVITY REGULATION: Lipase activity is maximal at a lipid-water interface (interfacial activation), probably by an induced conformational change that results in an increased accessibility of the active site to the substrate. |
| 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: Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:11334664, ECO:0000269|PubMed:7765029}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:11334664, ECO:0000269|PubMed:7765029}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (14); Chain (1); Disulfide bond (3); Helix (10); Metal binding (1); Mutagenesis (1); Propeptide (1); Region (1); Sequence conflict (2); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1LGY; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,139 |
| Kinetics | |
| Metal Binding | METAL 379; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |