| IED ID | IndEnz0005000493 |
| Enzyme Type ID | lipase000493 |
| Protein Name |
Pyrethroid hydrolase Ces2a EC 3.1.1.88 Carboxylic ester hydrolase EC 3.1.1.- |
| Gene Name | Ces2a Ces6 LOC246252 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MPLARLPGWLYVVACGLLLLLQHVHGQDSASPIRNTHTGQVRGSFVHVKDTKSGIHTFLGIPFAKPPVGPLRFAPPEDPEPWSGVRDATSQPAMCLQTDIMNLDGIKEMKLTVHPTPMSEDCLYLNIYTPAHAREGSNLPVMVWIHGGGLVLGSASMNDASTLAATEEIVIVSIQYRLGVLGFFSTGDQNARGNWGYLDQVAALRWVQQNIAYFGGNHGKVTIFGGSAGGTSVSSHVVSPMSKGLFHGAIMQSGVALLPDLISDKSEVVYKTVANLSGCEAPDSEALIRCLRAKSKQEILAINQVFKMIPGVVDGKFLPKHPQELLASGDFHPVPSIIGINTDECGWGIPVFLGLDHIIKKITRETLPTVLKSTAAQMMLPPECIDLIMEEYMGDTENPETLQEQFRHMLGDFMFVIPALQVAHFQRSQAPVYFYEFQHLPSFIKQVRPSHVKADHGDDILFVFGSYLWGMTFDLTEEEELLKRRVMKYWANFARTGNPNGEDLPHWPVLDHDEQYLQLNTQPAVGRALKARRLQFWTKTLPQKIQELKGSQSKHAEL |
| Enzyme Length | 558 |
| Uniprot Accession Number | Q8K3R0 |
| Absorption | |
| Active Site | ACT_SITE 227; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 344; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 456; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000269|PubMed:12230550};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000305|PubMed:12230550}; 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:0000250|UniProtKB:Q8QZR3}; |
| DNA Binding | |
| EC Number | 3.1.1.88; 3.1.1.- |
| Enzyme Function | FUNCTION: Carboxylesterases that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes permethrin faster than cypermethrin (By similarity). Hydrolyzes retinyl esters (PubMed:12230550). {ECO:0000250|UniProtKB:Q8QZR3, ECO:0000269|PubMed:12230550}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (2); Modified residue (1); Signal peptide (1) |
| Keywords | Alternative splicing;Disulfide bond;Endoplasmic reticulum;Hydrolase;Microsome;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}. |
| Modified Residue | MOD_RES 296; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q8QZR3 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255|RuleBase:RU361235 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 34503976; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,802 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 0.05 min(-1) with retinyl palmitate as substrate. {ECO:0000269|PubMed:12230550}; |
| Metal Binding | |
| Rhea ID | RHEA:13933; RHEA:13934; RHEA:30283 |
| Cross Reference Brenda | 3.1.1.1; |