Acetylcholinesterase (ACHE; EC 3.1.1.7) controls synaptic and neurohumoral cholinergic activity by hydrolyzing the neurotransmitter acetylcholine. ACHE function relies on precise regulation of its expression and localization. In particular, alternative splicing of the 3-prime region of ACHE results in ACHE isoforms with distinct C-terminal peptides that determine posttranslational maturation and oligomeric assembly
Interpro : IPR000997 Cholinesterase , IPR002018 Carboxylesterase, type B
PIRSF : PIRSF005676 COesterase
Pdoc : No Pdoc
Pfam : PF00135 COesterase
Prints : PR00878
EC Number : No EC Number
Peptide in | Fasta |
Nucleotide in | Fasta |
Alignment with Multalin | Text only |
Seed alignment with MAFFT | No colour / coloured with Mview |
Alignment with MAFFT | No colour / coloured with Mview |
Dendrogram | The dnd file |
Substrate | Chemical Nomenclature | Proteins |
---|---|---|
Acetylcholine | 2-(Acetyloxy)-N,N,N,-trimethylethanaminium | bunfa-ACHE eleel-ACHE chick-ACHE human-ACHE human-BCHE mouse-ACHE mouse-BCHE ratno-ACHE torca-ACHE torma-ACHE |
Acetylthiocholine | 2-acetylsulfanylethyl(trimethyl)azanium | bunfa-ACHE eleel-ACHE chick-ACHE human-ACHE human-BCHE mouse-ACHE mouse-BCHE ratno-ACHE torca-ACHE torma-ACHE |
O-Nitrophenylacetate | (2-nitrophenyl) acetate |
Inhibitor | Chemical Nomenclature | Proteins |
---|---|---|
11a-quinoxaline | N-(3-aminoquinoxalin-2-yl)-4-(piperidin-1-ylmethyl)benzamide | |
18-E100 | 1-[7-(4-chlorophenoxy)heptyl]azepane | |
BYYT-25 | 5,6-dimethoxy-2-[4-(pyrrolidin-1-ylmethyl)phenoxy]-2,3-dihydroinden-1-one | |
Canadine | 16,17-dimethoxy-5,7-dioxa-13-azapentacyclo[11.8.0.02,10.04,8.015,20]henicosa-2,4(8),9,15(20),16,18-hexaene | |
Methylene-blue-carboline-2 | 1-[3,7-bis(dimethylamino)phenothiazin-10-yl]-3-(2-ethyl-3,4-dihydro-1H-pyrido[4,3-b]indol-5-yl)propan-1-one | |
Thalictricavine | (1R,21S)-16,17-dimethoxy-21-methyl-5,7-dioxa-13-azapentacyclo[11.8.0.02,10.04,8.015,20]henicosa-2,4(8),9,15(20),16,18-hexaene | |
UW-MD-71 | (7-(3-(piperidin-1-yl)propoxy)-1,2,3,9-tetrahydropyrrolo[2,1-b]quinazoline |
Title : Old and new questions about cholinesterases - Massoulie_2008_Chem.Biol.Interact_175_30 |
Author(s) : Massoulie J , Perrier N , Noureddine H , Liang D , Bon S |
Ref : Chemico-Biological Interactions , 175 :30 , 2008 |
Abstract : |
PubMedSearch : Massoulie_2008_Chem.Biol.Interact_175_30 |
PubMedID: 18541228 |
Title : The cholinesterases: from genes to proteins - Taylor_1994_Annu.Rev.Pharmacol.Toxicol_34_281 |
Author(s) : Taylor P , Radic Z |
Ref : Annual Review of Pharmacology & Toxicology , 34 :281 , 1994 |
Abstract : |
PubMedSearch : Taylor_1994_Annu.Rev.Pharmacol.Toxicol_34_281 |
PubMedID: 8042853 |
Title : Molecular and cellular biology of cholinesterases - |
Author(s) : Massoulie J , Pezzementi L , Bon S , Krejci E , Vallette FM |
Ref : Prog Neurobiol , 41 :31 , 1993 |
PubMedID: 8321908 |
Title : Comparison of butyrylcholinesterase and acetylcholinesterase. - |
Author(s) : Chatonnet A , Lockridge O |
Ref : Biochemical Journal , 260 :625 , 1989 |
PubMedID: 2669736 |