| IED ID | IndEnz0010000117 |
| Enzyme Type ID | esterase000117 |
| Protein Name |
Esterase TesA EC 3.1.1.1 |
| Gene Name | tesA PA2856 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MRALLLSGCLALVLLTQQAAAQTLLVVGDSISAALGLDTSQGWVALLQKRLADEGYDYRVVNASISGDTSAGGLARLPALLAEEKPALVVIELGGNDGLRGMAPAQLQQNLASMAQKARAEGAKVLLLGIQLPPNYGPRYIEAFSRVYGAVAAQEKTALVPFFLEGVGGVQGMMQADGIHPALAAQPRLLENVWPTLKPLL |
| Enzyme Length | 201 |
| Uniprot Accession Number | Q9HZY8 |
| Absorption | |
| Active Site | ACT_SITE 30; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 177; /evidence=ECO:0000250; ACT_SITE 180; /evidence=ECO:0000250 |
| 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:20931591}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Esterase that exhibits the highest activity towards Tween detergents and p-nitrophenyl esters of short acyl chain length. Also displays a low thioesterase activity towards palmitoyl-coenzyme A, but is not active towards acetyl-coenzyme A. {ECO:0000269|PubMed:20931591}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (6); Chain (1); Helix (11); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4JGG; |
| Mapped Pubmed ID | 23874889; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,038 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.0 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591}; Vmax=37 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate {ECO:0000269|PubMed:20931591}; |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda |