| IED ID | IndEnz0005000212 |
| Enzyme Type ID | lipase000212 |
| Protein Name |
Acetylcholinesterase 1 ACE-1 AChE 1 EC 3.1.1.7 |
| Gene Name | ace-1 W09B12.1 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MRNSLLFFIFLPSTILAVDLIHLHDGSPLFGEEVLSQTGKPLTRFQGIPFAEPPVGNLRFKKPKPKQPWRIPLNATTPPNSCIQSEDTYFGDFYGSTMWNANTKLSEDCLYLNVYVPGKVDPNKKLAVMVWVYGGGFWSGTATLDVYDGRILTVEENVILVAMNYRVSIFGFLYMNRPEAPGNMGMWDQLLAMKWVHKNIDLFGGDLSRITLFGESAGAASVSIHMLSPKSAPYFHRAIIQSGSATSPWAIEPRDVALARAVILYNAMKCGNMSLINPDYDRILDCFQRADADALRENEWAPVREFGDFPWVPVVDGDFLLENAQTSLKQGNFKKTQLLAGSNRDESIYFLTYQLPDIFPVADFFTKTDFIKDRQLWIKGVKDLLPRQILKCQLTLAAVLHEYEPQDLPVTPRDWINAMDKMLGDYHFTCSVNEMALAHTKHGGDTYYYYFTHRASQQTWPEWMGVLHGYEINFIFGEPLNQKRFNYTDEERELSNRFMRYWANFAKTGDPNKNEDGSFTQDVWPKYNSVSMEYMNMTVESSYPSMKRIGHGPRRKECAFWKAYLPNLMAAVADVGDPYLVWKQQMDKWQNEYITDWQYHFEQYKRYQTYRQSDSETCGG |
| Enzyme Length | 620 |
| Uniprot Accession Number | P38433 |
| Absorption | |
| Active Site | ACT_SITE 216; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 346; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 468; /note=Charge relay system; /evidence=ECO:0000250 |
| 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:0000305|PubMed:8144590};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562; Evidence={ECO:0000305|PubMed:8144590}; |
| DNA Binding | |
| EC Number | 3.1.1.7 |
| Enzyme Function | FUNCTION: Rapidly hydrolyzes acetylcholine and releases choline into the synapse (Probable). It can hydrolyze propionylcholine and butyrylthiocholine in vitro (Probable). {ECO:0000305|PubMed:8144590}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (4); Glycosylation (4); Signal peptide (1) |
| Keywords | Cell junction;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Neurotransmitter degradation;Reference proteome;Secreted;Serine esterase;Signal;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}. Note=May be secreted or membrane associated via a non-catalytic subunit. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10438595; 10778742; 10891266; 11381264; 11580201; 12097347; 12911746; 16243303; 17164286; 19343510; 20439776; 21177967; 21515580; 22267497; 22347378; 22560298; 23800452; 24884423; 25487147; 28545126; 3272166; 4020534; 6593563; 7274654; 7274655; 7835425; |
| Motif | |
| Gene Encoded By | |
| Mass | 71,433 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57 uM for acetylthiocholine {ECO:0000269|PubMed:8144590}; |
| Metal Binding | |
| Rhea ID | RHEA:17561; RHEA:17562 |
| Cross Reference Brenda |