| IED ID | IndEnz0005000993 |
| Enzyme Type ID | lipase000993 |
| Protein Name |
Acetylcholinesterase AChE EC 3.1.1.7 Cleaved into: Acetylcholinesterase 16 kDa subunit; Acetylcholinesterase 55 kDa subunit |
| Gene Name | Ace CG17907 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEIGKALINDCNCNASMLKTNPAHVMSCMRSVDAKTISVQQWNSYSGILSFPSAPTIDGAFLPADPMTLMKTADLKDYDILMGNVRDEGTYFLLYDFIDYFDKDDATALPRDKYLEIMNNIFGKATQAEREAIIFQYTSWEGNPGYQNQQQIGRAVGDHFFTCPTNEYAQALAERGASVHYYYFTHRTSTSLWGEWMGVLHGDEIEYFFGQPLNNSLQYRPVERELGKRMLSAVIEFAKTGNPAQDGEEWPNFSKEDPVYYIFSTDDKIEKLARGPLAARCSFWNDYLPKVRSWAGTCDGDSGSASISPRLQLLGIAALIYICAALRTKRVF |
| Enzyme Length | 649 |
| Uniprot Accession Number | P07140 |
| Absorption | |
| Active Site | ACT_SITE 276; /note=Acyl-ester intermediate; ACT_SITE 405; /note=Charge relay system; ACT_SITE 518; /note=Charge relay system |
| 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; |
| DNA Binding | |
| EC Number | 3.1.1.7 |
| Enzyme Function | FUNCTION: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (21); Chain (3); Disulfide bond (4); Glycosylation (4); Helix (28); Lipidation (1); Mutagenesis (7); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Cell junction;Cell membrane;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Neurotransmitter degradation;Reference proteome;Serine esterase;Signal;Synapse |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell junction, synapse. Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell. {ECO:0000269|PubMed:2975507}.; PTM: Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion. {ECO:0000269|PubMed:1730712}. |
| Signal Peptide | SIGNAL 1..38 |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1DX4; 1QO9; 1QON; 6XYS; 6XYU; 6XYY; |
| Mapped Pubmed ID | 10021768; 10421447; 10421448; 10470487; 10580988; 10766776; 11136231; 11170446; 11252751; 11278288; 11286337; 11842237; 11888271; 12486703; 12696670; 12888516; 12944426; 1310468; 1412713; 14239786; 14504029; 14507965; 15018650; 15018651; 15020472; 15030487; 15036810; 1520255; 15266379; 15469930; 15588702; 15666354; 1573390; 1582561; 15875013; 15972463; 16023296; 16083272; 16100272; 1611033; 1629220; 16408306; 16453566; 1648000; 16686937; 1679453; 16814731; 17002944; 17246310; 1731068; 17355286; 1736311; 1747098; 17625558; 18056427; 18422651; 18439026; 18463699; 18493064; 18514176; 18550751; 18555981; 18570631; 18602377; 18644713; 18663432; 18959482; 19263097; 19559912; 19649249; 20220848; 20236518; 20371351; 20585551; 20936265; 21074052; 2108864; 21105647; 2120047; 2124571; 21305389; 21391508; 2155155; 21940169; 22365130; 22521218; 22579458; 23071443; 23170910; 23475318; 23500627; 23583979; 23608486; 23904743; 24039837; 24173775; 24231732; 24324170; 24555652; 24637386; 24972496; 25000897; 2511423; 25193493; 25242144; 25312911; 25345443; 25435894; 25644700; 25687947; 25706129; 25824290; 26033662; 26117601; 26302912; 26366809; 26460970; 26526100; 26564900; 26581847; 2660188; 26637434; 26931800; 27098909; 27146270; 27174135; 27317781; 27701059; 27725363; 27794539; 27920150; 28202685; 2826288; 28267671; 28273459; 28369070; 2840338; 28849357; 28950660; 2904861; 29080449; 2912799; 29191452; 29228179; 29653138; 29723993; 30178145; 30190420; 30190421; 30366679; 30385770; 30478906; 30479347; 30510719; 30516209; 30930439; 31054025; 3115978; 3121787; 3123293; 3123888; 31376529; 3141264; 31422521; 31585867; 31677527; 31867121; 31975175; 32025502; 32155891; 32279006; 32344153; 32392293; 32493733; 32496927; 32524642; 32691858; 32759552; 32865393; 32905187; 32930862; 33121485; 33212211; 33350518; 33384590; 33514461; 33533492; 33540716; 33555999; 33576765; 33635910; 33675736; 33716020; 33719225; 33777703; 33827210; 33920660; 33992327; 3856864; 5456437; 6224022; 6312055; 6410077; 6413654; 6437902; 6769980; 6776006; 6790339; 6807282; 7599628; 7794239; 8005411; 8016090; 8028587; 8074730; 8119594; 821817; 8384578; 8730102; 8730103; 8890157; 9023722; 9187243; 9393432; 9409831; 9425116; 9452390; 9518457; 9597732; 9627407; 9629668; 9862431; |
| Motif | |
| Gene Encoded By | |
| Mass | 71,785 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17561 |
| Cross Reference Brenda | 3.1.1.7; |