IED ID | IndEnz0010000333 |
Enzyme Type ID | esterase000333 |
Protein Name |
Acetylcholinesterase AChE EC 3.1.1.7 Fragment |
Gene Name | ACE-1 |
Organism | Culex torrentium (Mosquito) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Nematocera Culicomorpha Culicoidea Culicidae (mosquitos) Culicinae Culicini Culex Culex Culex torrentium (Mosquito) |
Enzyme Sequence | SGKKVDAWMGIPYAQPPLGPLRFRHPRPAERWTGVLNATKPPNSCVQIVDTVFGDFPGATMWNPNTPLSEDCLYINVVVPRPRPKNAAVMLWIFGGGFYSGTATLDVYDHRTLASEENVIVVSLQYRVASLG |
Enzyme Length | 132 |
Uniprot Accession Number | Q86GC9 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7; Evidence={ECO:0000250|UniProtKB:P22303}; |
DNA Binding | |
EC Number | 3.1.1.7 |
Enzyme Function | FUNCTION: Rapidly hydrolyzes choline released into the synapse. {ECO:0000305}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Glycosylation (1); Non-terminal residue (2) |
Keywords | Cell junction;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Neurotransmitter degradation;Secreted;Serine esterase;Synapse |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. Secreted {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 14,543 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:17561 |
Cross Reference Brenda |