IED ID | IndEnz0010000199 |
Enzyme Type ID | esterase000199 |
Protein Name |
Acetylcholinesterase AChE EC 3.1.1.7 Fragments |
Gene Name | ACHE |
Organism | Naja oxiana (Central Asian cobra) (Oxus cobra) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Elapidae Elapinae Naja Naja oxiana (Central Asian cobra) (Oxus cobra) |
Enzyme Sequence | SELKVATQTGFVRGLSLPVLAGHVSAHLGVPFAEPFLRPEPVKPGAEMWNPNLNIWVPSGRVGAFXFLTVTLFGESAGAASVGMXLLSTQRAILQSGAPNAPWAQVQPAESRFPFVPVIDGEFFPLGVNKDEGSFGVPGFSKXXESLINQAVPHANDIYTDWQDQDNGGLPLTGNPTXPHN |
Enzyme Length | 181 |
Uniprot Accession Number | Q7LZG1 |
Absorption | |
Active Site | ACT_SITE 76; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 132; /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:0000250|UniProtKB:Q92035}; |
DNA Binding | |
EC Number | 3.1.1.7 |
Enzyme Function | FUNCTION: In venom, its toxic role is unclear: it could result in less musculatory control by rapidly hydrolyzing acetylcholine, or that it works synergistically with alkaline phosphatase (ALP) in paralyzing prey through hypotension. In muscle, it terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. In liver, its function is unclear: it could serve as a safeguard against any diffusion of acetylcholine from synapses into the circulation. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Non-adjacent residues (12); Non-terminal residue (2); Region (1) |
Keywords | Cell junction;Cell membrane;Direct protein sequencing;Hydrolase;Membrane;Neurotransmitter degradation;Secreted;Serine esterase;Synapse;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 19,255 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:17561 |
Cross Reference Brenda |