| IED ID | IndEnz0005000494 |
| Enzyme Type ID | lipase000494 |
| Protein Name |
Pyrethroid hydrolase Ces2e EC 3.1.1.88 Carboxylic ester hydrolase EC 3.1.1.- carboxylesterase 2E |
| Gene Name | Ces2e Ces5 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MPLYKLLGWLNAVACGVLLLVLHVQGQDSASPIRNTHTGQVRGSLVHVKDTDIAVHTFLGIPFAKPPVGPLRFAPPEAPEPWSGVRDGTSHPNMCLQNDNLMGSEDLKMMNLILPPISMSEDCLYLNIYVPAHAHEGSNLPVMVWIHGGALTVGMASMYDGSMLAATEDVVVVAIQYRLGVLGFFSTGDQHAKGNWGYLDQVAALRWVQQNIVHFGGNPDRVTIFGESAGGTSVSSHVVSPMSQGLFHGAIMESGVAVLPDLISSSSEMVHRIVANLSGCAAVNSETLMCCLRGKNEAEMLAINKVFKIIPGVVDGEFLPKHPQELMASKDFHPVPSIIGINNDEYGWILPTIMDPAQKIEEITRKTLPAVLKSTALKMMLPPECGDLLMEEYMGDTEDPETLQAQFREMKGDFMFVIPALQVAHFQRSHAPVYFYEFQHRPSFFKDFRPPYVKADHGDEIFLVFGYQFGNIKLPYTEEEEQLSRRIMKYWANFARHGNPNSEGLPYWPVMDHDEQYLQLDIQPSVGRALKARRLQFWTKTLPQKIQELKGSQERHKEL |
| Enzyme Length | 559 |
| Uniprot Accession Number | Q8BK48 |
| Absorption | |
| Active Site | ACT_SITE 228; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 345; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 457; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141 |
| 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:15123619}; 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:0000250|UniProtKB:G3V7J5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000250|UniProtKB:G3V7J5}; |
| 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. Hydrolyzes retinyl esters (By similarity). {ECO:0000250|UniProtKB:G3V7J5, ECO:0000269|PubMed:15123619}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (1); Modified residue (2); Sequence conflict (3); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Microsome;Phosphoprotein;Pyrrolidone carboxylic acid;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:15123619}. |
| Modified Residue | MOD_RES 27; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P14943; MOD_RES 552; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17208939 |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:15123619}. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:15123619 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 14681479; 16615898; 17205597; 20931200; 21267068; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,318 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=286 uM for p-Nitrophenyl acetate {ECO:0000269|PubMed:15123619}; KM=0.5 uM for cypermethrin {ECO:0000269|PubMed:15123619}; KM=2.2 uM for (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R/S)-trans/cis-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropane carboxylate {ECO:0000269|PubMed:15123619}; KM=0.89 uM for (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R)-(-)-2-(4-chlorophenyl)-3-methyl butanoate ((alphaR/S)(2R)-A3) {ECO:0000269|PubMed:15123619}; KM=0.96 uM for chrysanthemic acid {ECO:0000269|PubMed:15123619}; Note=kcat is 94 sec(-1) with p-Nitrophenyl acetate as substrate. kcat is 0.12 sec(-1) with cypermethrin as substrate. kcat is 0.11 sec(-1) with (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R/S)-trans/cis-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropane carboxylate as substrate. kcat is 0.067 sec(-1) with (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R)-(-)-2-(4-chlorophenyl)-3-methyl butanoate ((alphaR/S)(2R)-A3) as substrate. kcat is 0.099 sec(-1) with chrysanthemic acid as substrate.; |
| Metal Binding | |
| Rhea ID | RHEA:30283; RHEA:13933; RHEA:13934 |
| Cross Reference Brenda | 3.1.1.1; |