| IED ID | IndEnz0018000058 |
| Enzyme Type ID | peroxidase000058 |
| Protein Name |
Arylesterase EC 3.1.1.2 Aryl-ester hydrolase Carboxylic acid perhydrolase PFE Putative bromoperoxidase EC 1.-.-.- |
| Gene Name | estF |
| Organism | Pseudomonas fluorescens |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas fluorescens group (fluorescent pseudomonads) Pseudomonas fluorescens |
| Enzyme Sequence | MSTFVAKDGTQIYFKDWGSGKPVLFSHGWLLDADMWEYQMEYLSSRGYRTIAFDRRGFGRSDQPWTGNDYDTFADDIAQLIEHLDLKEVTLVGFSMGGGDVARYIARHGSARVAGLVLLGAVTPLFGQKPDYPQGVPLDVFARFKTELLKDRAQFISDFNAPFYGINKGQVVSQGVQTQTLQIALLASLKATVDCVTAFAETDFRPDMAKIDVPTLVIHGDGDQIVPFETTGKVAAELIKGAELKVYKDAPHGFAVTHAQQLNEDLLAFLKR |
| Enzyme Length | 272 |
| Uniprot Accession Number | P22862 |
| Absorption | |
| Active Site | ACT_SITE 95; /evidence=ECO:0000305|PubMed:15213385; ACT_SITE 223; /evidence=ECO:0000305|PubMed:15213385; ACT_SITE 252; /evidence=ECO:0000305|PubMed:15213385 |
| Activity Regulation | |
| Binding Site | BINDING 29; /note="Acetate"; /evidence="ECO:0000269|PubMed:20112920, ECO:0007744|PDB:3HI4"; BINDING 96; /note="Acetate"; /evidence="ECO:0000269|PubMed:20112920, ECO:0007744|PDB:3HI4" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:1368608, ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:7704276, ECO:0000269|PubMed:9571805}; CATALYTIC ACTIVITY: Reaction=H2O + peracetic acid = acetate + H(+) + H2O2; Xref=Rhea:RHEA:68392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:30089, ChEBI:CHEBI:42530; Evidence={ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:20112920}; CATALYTIC ACTIVITY: Reaction=a percarboxylic acid + H2O = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:68396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29067, ChEBI:CHEBI:177878; Evidence={ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:20112920, ECO:0000269|PubMed:22618813}; |
| DNA Binding | |
| EC Number | 3.1.1.2; 1.-.-.- |
| Enzyme Function | FUNCTION: Hydrolyzes phenolic esters, such as phenyl acetate, nitrophenyl acetate and naphtyl acetate (PubMed:1368608, PubMed:7704276, PubMed:9571805, PubMed:15803517). Can act on a wide range of esters, but reaction rate and enantioselectivity differ significantly depending on the substrate (PubMed:1368608, PubMed:9571805). Shows a preference for esters with small acyl groups (PubMed:15213385). Also shows low perhydrolase activity, and catalyzes the reversible formation of peroxycarboxylic acids from carboxylic acids and hydrogen peroxide (PubMed:15803517, PubMed:20112920, PubMed:22618813). In vitro, enzyme-generated peracetic acid oxidizes bromide ion to bromonium, which reacts with monochlorodimedone to form bromochlorodimedone (PubMed:7704276, PubMed:20112920, PubMed:22618813). {ECO:0000269|PubMed:1368608, ECO:0000269|PubMed:15213385, ECO:0000269|PubMed:15803517, ECO:0000269|PubMed:20112920, ECO:0000269|PubMed:22618813, ECO:0000269|PubMed:7704276, ECO:0000269|PubMed:9571805}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius for esterase activity. {ECO:0000269|PubMed:7704276}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is above 9.0 for esterase activity. {ECO:0000269|PubMed:7704276}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (8); Binding site (2); Chain (1); Domain (1); Frameshift (1); Helix (13); Initiator methionine (1); Mutagenesis (8); Turn (1) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Oxidoreductase;Peroxidase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1VA4; 3HEA; 3HI4; 3IA2; 3T4U; 3T52; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,092 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:7704276}; KM=2.8 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:15803517}; KM=33 mM for ethyl acetate {ECO:0000269|PubMed:20112920}; KM=43 mM for methyl acetate {ECO:0000269|PubMed:20112920}; KM=60 mM for methyl acetate {ECO:0000269|PubMed:22618813}; KM=0.041 mM for peracetic acid {ECO:0000269|PubMed:20112920}; KM=500 mM for acetic acid {ECO:0000269|PubMed:20112920}; KM=3.3 mM for hydrogen peroxide {ECO:0000269|PubMed:20112920}; KM=17 mM for H(2)O(2) {ECO:0000269|PubMed:15803517}; Note=kcat is 9 sec(-1) with ethyl acetate as substrate. kcat is 25 sec(-1) with methyl acetate as substrate. kcat is 100 sec(-1) with peracetic acid as substrate. kcat is 0.12 sec(-1) with acetic acid as substrate. kcat is 0.094 sec(-1) with hydrogen peroxide as substrate (PubMed:20112920). kcat is 15 sec(-1) with methyl acetate as substrate (PubMed:22618813). {ECO:0000269|PubMed:20112920, ECO:0000269|PubMed:22618813}; |
| Metal Binding | |
| Rhea ID | RHEA:17309; RHEA:68392; RHEA:68396 |
| Cross Reference Brenda |