| IED ID | IndEnz0010001522 |
| Enzyme Type ID | esterase001522 |
| Protein Name |
Pyrethroid hydrolase EC 3.1.1.88 |
| Gene Name | pytH |
| Organism | Sphingobium wenxiniae (strain DSM 21828 / JZ-1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Sphingomonadales Sphingomonadaceae Sphingobium Sphingobium wenxiniae (strain DSM 21828 / JZ-1) |
| Enzyme Sequence | MTVTDIILIHGALNRGACYDAVVPLLEARGYRVHAPDLTGHTPGDGGHLSVVDMEHYTRPVADILARAEGQSILLGHSLGGASISWLAQHHPDKVAGLIYLTAVLTAPGITPETFVLPGEPNRGTPHALDLIQPVDEGRGLQADFSRLERLREVFMGDYPGEGMPPAEQFIQTQSTVPFGTPNPMEGRALEIPRLYIEALDDVVIPIAVQRQMQKEFPGPVAVVSLPASHAPYYSMPERLAEAIADFADAPAEYRQTATKAGPDRPAGADGGRADRADLP |
| Enzyme Length | 280 |
| Uniprot Accession Number | C0LA90 |
| Absorption | |
| Active Site | ACT_SITE 202; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 230; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| 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:19581484}; |
| DNA Binding | |
| EC Number | 3.1.1.88 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of pyrethroids pesticides. Catalyzes the hydrolysis of cypermethrin to equimolar amounts of cyano-3-phenoxybenzyl alcohol and 2,2-dimethyl-3-(2,2-dichlorovinyl)-cyclopropanecarboxylic acid. Hydrolyzes cis-permethrin at approximately equal rate to trans-permethrin. {ECO:0000269|PubMed:19581484}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:19581484}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Region (1) |
| Keywords | 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 | 30,012 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.062 uM for trans-Permethrin {ECO:0000269|PubMed:19581484}; KM=0.065 uM for cis-Permethrin {ECO:0000269|PubMed:19581484}; KM=0.106 uM for Fenpropathrin {ECO:0000269|PubMed:19581484}; KM=0.110 uM for trans-Cypermethrin {ECO:0000269|PubMed:19581484}; KM=0.108 uM for cis-Cypermethrin {ECO:0000269|PubMed:19581484}; KM=0.348 uM for Cyhalothrin {ECO:0000269|PubMed:19581484}; KM=0.585 uM for Fenvalerate {ECO:0000269|PubMed:19581484}; KM=0.788 uM for Deltamethrin {ECO:0000269|PubMed:19581484}; KM=1.586 uM for Bifenthrin {ECO:0000269|PubMed:19581484}; KM=124 uM for p-Nitrophenyl acetate {ECO:0000269|PubMed:19581484}; KM=176 uM for p-Nitrophenyl butyrate {ECO:0000269|PubMed:19581484}; KM=325 uM for p-Nitrophenyl caproate {ECO:0000269|PubMed:19581484}; Note=kcat is 3.03 sec(-1) with trans-Permethrin acetate as substrate. kcat is 3.00 sec(-1) with cis-Permethrin acetate as substrate. kcat is 2.61 sec(-1) with Fenpropathrin acetate as substrate. kcat is 2.53 sec(-1) with trans-Cypermethrin acetate as substrate. kcat is 2.57 sec(-1) with cis-Cypermethrin acetate as substrate. kcat is 1.28 sec(-1) with Cyhalothrin acetate as substrate. kcat is 0.91 sec(-1) with Fenvalerate acetate as substrate. kcat is 0.79 sec(-1) with Deltamethrin acetate as substrate. kcat is 0.44 sec(-1) with Bifenthrin acetate as substrate. kcat is 183 sec(-1) with p-Nitrophenyl acetate as substrate. kcat is 118 sec(-1) with p-Nitrophenyl butyrate acetate as substrate. kcat is 49 sec(-1) with p-Nitrophenyl caproate acetate as substrate.; |
| Metal Binding | |
| Rhea ID | RHEA:30283 |
| Cross Reference Brenda | 3.1.1.88; |