| IED ID | IndEnz0005001399 |
| Enzyme Type ID | lipase001399 |
| Protein Name |
Lipase EstA Lipase A EC 3.1.1.3 Triacylglycerol lipase |
| Gene Name | estA lip lipA BSU02700 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MKFVKRRIIALVTILMLSVTSLFALQPSAKAAEHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNGPVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTLGGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIHGVGHIGLLYSSQVNSLIKEGLNGGGQNTN |
| Enzyme Length | 212 |
| Uniprot Accession Number | P37957 |
| Absorption | |
| Active Site | ACT_SITE 108; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437"; ACT_SITE 164; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437"; ACT_SITE 187; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437" |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited when incubated with the serine reagent phenylmethylsulfonyl fluoride. Activated by the addition of calcium to the reaction mixture. When calcium was incubated with the lipase but not added to the reaction mixture, its effect is lower but still observable. Magnesium, manganese and strontium are not able to replace calcium with full retention of activity. {ECO:0000269|PubMed:8396026}. |
| 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|PubMed:11029590, ECO:0000269|PubMed:8396026}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Active toward triacylglycerides with a preference for esters with C8:0 acyl groups; barely active on C18:1 or C18:4 substrates. Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18. {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:8396026, ECO:0000305|PubMed:1320940}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. Stable for at least 30 minutes at 40 degrees Celsius. Virtually no activity remains after 30 minutes at 55 degrees Celsius. {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:8396026}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10 (PubMed:11029590). The activity decreases strongly above pH 10.5 or below pH 6.5. The enzyme is remarkably stable at alkaline pH, showing maximum stability at pH 12 and retaining more than 65% of its activity after 24 hours at pH 13 (PubMed:8396026). {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:8396026}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (7); Chain (1); Helix (10); Sequence conflict (5); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Maximally expressed in late exponential growth phase. Expression decreases rapidly in the stationary phase. Expressed in both rich and minimal media with glucose as carbon source (at protein level). {ECO:0000269|PubMed:11583117, ECO:0000269|PubMed:8396026}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11583117, ECO:0000269|PubMed:8396026}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000305|PubMed:8396026 |
| Structure 3D | X-ray crystallography (21) |
| Cross Reference PDB | 1I6W; 1ISP; 1R4Z; 1R50; 1T2N; 1T4M; 2QXT; 2QXU; 3D2A; 3D2B; 3D2C; 3QMM; 3QZU; 5CRI; 5CT4; 5CT5; 5CT6; 5CT8; 5CT9; 5CTA; 5CUR; |
| Mapped Pubmed ID | 14684916; 15321721; 16342303; 18053819; 18599073; 21925508; 22267088; 26388426; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,791 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |