| IED ID | IndEnz0010000115 |
| Enzyme Type ID | esterase000115 |
| Protein Name |
Carboxylesterase EC 3.1.1.1 |
| Gene Name | est est30 |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MKIVPPKPFFFEAGERAVLLLHGFTGNSADVRMLGRFLESKGYTCHAPIYKGHGVPPEELVHTGPDDWWQDVMNGYEFLKNKGYEKIAVAGLSLGGVFSLKLGYTVPIEGIVTMCAPMYIKSEETMYEGVLEYAREYKKREGKSEEQIEQEMEKFKQTPMKTLKALQELIADVRDHLDLIYAPTFVVQARHDEMINPDSANIIYNEIESPVKQIKWYEQSGHVITLDQEKDQLHEDIYAFLESLDW |
| Enzyme Length | 246 |
| Uniprot Accession Number | Q06174 |
| Absorption | |
| Active Site | ACT_SITE 93; /note=Nucleophile; ACT_SITE 192; /note=Charge relay system; ACT_SITE 222; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:15033540}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Involved in the detoxification of xenobiotics. Shows maximal activity with C6 substrates, with gradually decreasing activity from C8 to C12 substrates. No activity for higher chain length substrates acids rather than long-chain ones. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:15033540}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:15033540}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Erroneous initiation (2); Helix (11) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1R1D; 1TQH; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,256 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.16 uM for p-nitrophenyl caproate (at 60 degrees Celsius) {ECO:0000269|PubMed:15033540}; |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda | 3.1.1.1; |