| IED ID | IndEnz0005001461 |
| Enzyme Type ID | lipase001461 |
| Protein Name |
Pyrethroid hydrolase Ces2e EC 3.1.1.88 Carboxylic ester hydrolase EC 3.1.1.- |
| Gene Name | Ces2e |
| 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 | MAQTRAWKSIMPLESLPGWLNAVVWGLLLLFCQVQGQDSASPIRNTHTGQVRGSFVHVKDTKSGVHTFLGIPFAKPPIGPLRFAPPEPPEPWSGVRDGTSHPAMCLQNIDGLNLENLKIKMSRSPVSMSEDCLYLSIYTPAHTHKDSNLPVMVWIHGGGLCWGMASTYDGSMLAAIEDVVVVTIQYRLGILGFFSTGDEHARGNWGYLDQVAALRWVQQNIVHFGGNPDRVTIFGESAGGISVSSHVVSPMSQGLFHGAIMESGVALLPNLISNTSEVIYTMVANLSGCEPVDSEALMSCLREKSEEEMLAINNIVRTISGVVDGKFLPRHPLELLASVDFHPVPSIIGINSDEYGWIIPMLHPDSTMKEINRETMRAVLKNTAVQMMLPPECSDLLMEEYMGDTEDSKTLQIQFNEMMGDFIFVIPALQVAHFQRSHAPVYFYEFQHQSNFLKDIRPPHVKADHGDELPYVIGYLFWDMKFVFTEEEKLLSRKMIKYWANFARHGNPNSEGLPYWPALDHDEQYLQLDIQPVVGRALKARRLKFWTKTLPQKIQELKGSQDNHTEL |
| Enzyme Length | 567 |
| Uniprot Accession Number | G3V7J5 |
| Absorption | |
| Active Site | ACT_SITE 237; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 354; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 465; /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:Q8BK48}; |
| DNA Binding | |
| EC Number | 3.1.1.88; 3.1.1.- |
| Enzyme Function | FUNCTION: Carboxylesterase that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin. Also hydrolyzes trans-cypermethrin (By similarity). Hydrolyzes retinyl esters (PubMed:12230550). {ECO:0000250|UniProtKB:Q8BK48, ECO:0000269|PubMed:12230550}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Modified residue (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Disulfide bond;Endoplasmic reticulum;Hydrolase;Microsome;Pyrrolidone carboxylic acid;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}. |
| Modified Residue | MOD_RES 37; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P14943 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255|RuleBase:RU361235 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 63,583 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 0.27 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; |