| IED ID | IndEnz0005000869 |
| Enzyme Type ID | lipase000869 |
| Protein Name |
Lipase EC 3.1.1.3 Lip 42 Thermostable organic solvent tolerant lipase Triacylglycerol hydrolase |
| Gene Name | |
| Organism | Bacillus sp. |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. |
| Enzyme Sequence | MKCCRIMFVLLGLWFVFGLSVPGGRTEAASLRANDAPIVLLHGFTGWGREEMFGFKYWGGVRGDIEQWLNDNGYRTYTLAVGPLSSNWDRACEAYAQLVGGTVDYGAAHAAKHGHARFGRTYPGLLPELKRGGRIHIIAHSQGGQTARMLVSLLENGSQEEREYAKAHNVSLSPLFEGGHHFVLSVTTIATPHDGTTLVNMVDFTDRFFDLQKAVLEAAAVASNVPYTSQVYDFKLDQWGLRRQPGESFDHYFERLKRSPVWTSTDTARYDLSVSGAEKLNQWVQASPNTYYLSFSTERTYRGALTGNHYPELGMNAFSAVVCAPFLGSYRNPTLGIDDRWLENDGIVNTVSMNGPKRGSSDRIVPYDGTLKKGVWNDMGTYNVDHLEIIGVDPNPSFDIRAFYLRLAEQLASLRP |
| Enzyme Length | 416 |
| Uniprot Accession Number | Q5U780 |
| Absorption | |
| Active Site | ACT_SITE 141; /note=Nucleophile; /evidence=ECO:0000269|Ref.3; ACT_SITE 345; /note=Charge relay system; /evidence=ECO:0000269|Ref.3; ACT_SITE 386; /note=Charge relay system; /evidence=ECO:0000269|Ref.3 |
| Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by zinc and iron ions, and activated in vitro in 25% v/v DMSO and acetone. {ECO:0000269|Ref.1}. |
| 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; Evidence={ECO:0000269|Ref.1}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Triacylglycerol hydrolase that shows hydrolysis preference towards some of the natural oils such as olive, sunflower and corn oils. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Highly thermostable with a half-life of 315 minutes at 60 degrees Celsius, 125 minutes at 65 degrees Celsius and 45 minutes at 70 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Is stable in a broad pH range of 7-10. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (16); Chain (1); Helix (22); Metal binding (5); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Calcium;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4FKB; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,353 |
| Kinetics | |
| Metal Binding | METAL 314; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000269|Ref.3; METAL 385; /note=Calcium; /evidence=ECO:0000250; METAL 388; /note=Calcium; /evidence=ECO:0000269|Ref.3; METAL 393; /note=Calcium; /evidence=ECO:0000269|Ref.3; METAL 394; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000269|Ref.3 |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |