Detail Information for IndEnz0010000334
IED ID IndEnz0010000334
Enzyme Type ID esterase000334
Protein Name Acetylcholinesterase
AChE
EC 3.1.1.7
Gene Name ache
Organism Torpedo marmorata (Marbled electric ray)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Chondrichthyes Elasmobranchii (elasmobranchs) Batoidea (rays) Torpediniformes Torpedinidae (electric rays) Torpedo Torpedo marmorata (Marbled electric ray)
Enzyme Sequence MREMNLLVTSSLGVLLHLVVLCQADDDSELLVNTKSGKVMRTRIPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFPGSEMWNPNREMSEDCLYLNIWVPSPRPKSATVMLWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNMGLLDQRMALQWVHDNIQFFGGDPKTVTLFGESAGRASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELRRNLNCNLNSDEDLIQCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNAGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPIKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIFY
Enzyme Length 590
Uniprot Accession Number P07692
Absorption
Active Site ACT_SITE 224; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 351; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 464; /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;
DNA Binding
EC Number 3.1.1.7
Enzyme Function FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (4); Glycosylation (4); Lipidation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1)
Keywords Alternative splicing;Cell junction;Cell membrane;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Neurotransmitter degradation;Serine esterase;Signal;Synapse
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor. Cell junction, synapse.; SUBCELLULAR LOCATION: [Isoform T]: Cell membrane; Peripheral membrane protein. Cell junction, synapse. Note=Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.
Modified Residue
Post Translational Modification PTM: An interchain disulfide bond is present in what becomes position 596 of the T isoform. {ECO:0000250}.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000269|PubMed:3792544
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 66,744
Kinetics
Metal Binding
Rhea ID RHEA:17561
Cross Reference Brenda