| IED ID | IndEnz0010001749 |
| Enzyme Type ID | esterase001749 |
| Protein Name |
Pyrethroid hydrolase EC 3.1.1.88 |
| Gene Name | estP |
| Organism | Klebsiella sp. |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Klebsiella/Raoultella group Klebsiella unclassified Klebsiella Klebsiella sp. |
| Enzyme Sequence | MEICTKGSRKHLTSRASEPSYNVPENQYVLYVVSSTLSIVKQLVKVAESKKSRFSGAIEKLNERLDSLKDYRIINRDLVVKDLERLKKRFDTEVINAELSEQLAKINVNLSRSYSEKGYLRLEKATGSENEWWAKIKPSQNDDWQQFEPDGYTIFSSRDHYASLFKSYSDYEIEAKIPLPLRRGKAVVLYPEYISRICVLPESRSIQREQENFTKLRDKGIALSKKDWQAKLTTDELAEQEKERATINKRLGYFATEHEKVGIVHKALEPKLKPFQQIEKEWRQCKVKSKSTFPNSMTFVQNPAYQAVHSGFKKLKEQIGLADEDILLSLEKIEAIGLVNMPLLYERWCLLQIIKVLTQAFRYQPEDNWKRKLIANIQGNEEQISIQFFNPSVSRAITLQYEPFLANGKRPDFVLDVEAITKSGNQISKRLVVDAKYYSAAYLKQRGGIGGVIHELYNGKDYSECQENSVFVLHPVLDAVEKVVSPQEWAKDSYLGELSMFDWEPAHHQRQATNYGAVCANPMKSQRYLDEIQRMLGMFLQYGIEDNTSFRGASDDTHAVNFCVSCGSEKVVDVTKSMSSNNQKRWYRCNECTHFTVYTHCGTCNTRLIKNGEYWTYLSLMPMSSINIKCPNCESPV |
| Enzyme Length | 637 |
| Uniprot Accession Number | Q52NW7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Hg(2+), Ag(+) and rho-chloromercuribenzoate. {ECO:0000269|PubMed:16448191}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol + H(+); Xref=Rhea:RHEA:30283, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:62523, ChEBI:CHEBI:62527, ChEBI:CHEBI:62531; EC=3.1.1.88; Evidence={ECO:0000269|PubMed:16448191}; |
| DNA Binding | |
| EC Number | 3.1.1.88 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes cis-permethrin at approximately equal rate to trans-permethrin. {ECO:0000269|PubMed:16448191}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:16448191}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1) |
| Keywords | Direct protein sequencing;Hydrolase;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 73,427 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 uM for cis-permethrin {ECO:0000269|PubMed:16448191}; KM=0.11 uM for trans-permethrin {ECO:0000269|PubMed:16448191}; KM=0.21 uM for cypermethrin {ECO:0000269|PubMed:16448191}; KM=0.91 uM for fenvalerate {ECO:0000269|PubMed:16448191}; KM=1.23 uM for deltamethrin {ECO:0000269|PubMed:16448191}; KM=0.87 uM for malathion {ECO:0000269|PubMed:16448191}; Note=kcat is 1.05 sec(-1) with cis-permethrin as substrate. kcat is 1.14 sec(-1) with trans-permethrin as substrate. kcat is 0.288 sec(-1) with cypermethrin as substrate. kcat is 0.103 sec(-1) with fenvalerate as substrate. kcat is 0.016 sec(-1) with deltamethrin as substrate. kcat is 0.07 sec(-1) with malathion as substrate.; |
| Metal Binding | |
| Rhea ID | RHEA:30283 |
| Cross Reference Brenda | 3.1.1.1; |