| IED ID | IndEnz0010000089 |
| Enzyme Type ID | esterase000089 |
| Protein Name |
Extracellular esterase EstB EC 3.1.1.3 Extracellular esterase LipB Lipase B Triacylglycerol lipase |
| Gene Name | estB lipB yfiP BSU08350 |
| 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 | MKKVLMAFIICLSLILSVLAAPPSGAKAESVHNPVVLVHGISGASYNFFAIKNYLISQGWQSNKLYAIDFYDKTGNNLNNGPQLASYVDRVLKETGAKKVDIVAHSMGGANTLYYIKYLGGGNKIQNVVTLGGANGLVSSTALPGTDPNQKILYTSIYSLNDQIVINSLSRLQGARNIQLYGIGHIGLLSNSQVNGYIKEGLNGGGLNTN |
| Enzyme Length | 210 |
| Uniprot Accession Number | Q79F14 |
| Absorption | |
| Active Site | ACT_SITE 106; /note=Nucleophile; /evidence=ECO:0000305|PubMed:11029590; ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000305|PubMed:11029590; ACT_SITE 185; /note=Charge relay system; /evidence=ECO:0000305|PubMed:11029590 |
| 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; Evidence={ECO:0000269|PubMed:11029590}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: An esterase which preferentially hydrolyzes triacylglyceride substrates with short chain fatty acids (C3-C10) with the maximum activity towards tricaprylin (C8:0); essentially inactive on C18:1 or C18:4 substrates. Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18. {ECO:0000269|PubMed:11029590}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Stable up to 45 degrees Celsius. {ECO:0000269|PubMed:11029590}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 11-12. {ECO:0000269|PubMed:11029590}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Mutagenesis (4); Signal peptide (1) |
| Keywords | Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Induced in rich but not minimal media with glucose as carbon source (at protein level). Induced by growth on n-hexadecane and tributyrin. {ECO:0000269|PubMed:11583117}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:11583117}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000269|PubMed:11029590 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,363 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda | 3.1.1.23; |