| IED ID | IndEnz0010000040 |
| Enzyme Type ID | esterase000040 |
| Protein Name |
Acetylcholinesterase BfAChE EC 3.1.1.7 |
| Gene Name | ACHE |
| Organism | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
| 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 Bungarinae Bungarus Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
| Enzyme Sequence | MPSCQPGKMPAPWPWWLQLLLCIPSCVAVLPGRAGELKVSTQTGSVRGLSLPVLDGHVSAFLGIPFAEPPLGRMRFLRPEPVKPWQHVLDATSYKPACYQMVDTSYPGFQGTEMWNPNRGMSEDCLYLNIWVPSPRPKDAPVLVWIYGGGFYSGAASLDVYDGRFLTYTQNVILVSLSYRVGAFGFLGLPGSPEAPGNMGLLDQRLALQWIQNNIHPFGGNPRAVTVFGESAGAASVGMHLLSTQSRTLFQRAILQSGGPNAPWATVTPAESRGRAALLGKQLGCHFNNDSELVSCLRSKNPQELIDEEWSVLPYKSIFRFPFVPVIDGDFFPDTPEAMLSSGNFKETQVLLGVVKDEGSYFLIYGLPGFSKDNESLISRADFLEGVRMSVPHANDIATDAVVLQYTDWQDQDNREKNREALDDIVGDHNVICPVVQFANDYAKRNSKVYAYLFDHRASNLLWPPWMGVPHGYEIEFVFGLPLNDSLNYTPQEKELSRRMMRYWANFARTGNPTDPADKSGAWPTYTASQPQYVQLNTQPLATQPSLRAQICAFWNHFLPKLLNATDNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL |
| Enzyme Length | 606 |
| Uniprot Accession Number | Q92035 |
| Absorption | |
| Active Site | ACT_SITE 231; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 358; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 471; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by active site inhibitors: edrophonium, trimethyl-(m-acetamidopheny1)-ammonium iodide, and trimethyl-(p-acetarnidopheny1)-ammonium iodide (PubMed:4197660, PubMed:9187246). Inhibited by both active and peripheral site inhibitors: decamethonium, and BW284c51 (PubMed:8662867, PubMed:9187246). Inhibited by peripheral site inhibitors: snake acetylcholinesterase fasciculin-2, propidium, gallamine, D-tubocurarine, and tacrine (PubMed:8662867, PubMed:9187246, PubMed:25411244). Also inhibited by antibodies Elec410 and Fab410 (PubMed:25411244). {ECO:0000269|PubMed:25411244, ECO:0000269|PubMed:4197660, ECO:0000269|PubMed:8662867, ECO:0000269|PubMed:9187246}. |
| 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:0000269|PubMed:25411244, ECO:0000269|PubMed:4197660, ECO:0000269|PubMed:8674549, ECO:0000269|PubMed:9545320}; |
| DNA Binding | |
| EC Number | 3.1.1.7 |
| Enzyme Function | FUNCTION: 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. 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (22); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (25); Mutagenesis (2); Sequence conflict (2); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Alternative splicing;Cell junction;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Neurotransmitter degradation;Secreted;Serine esterase;Signal;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:0000269|PubMed:8674549}. |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4QWW; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,074 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=41.7 uM for acetylcholine (at pH 7.5) {ECO:0000269|PubMed:4197660}; KM=78.8 uM for acetylthiocholine (at pH 7.4) {ECO:0000269|PubMed:8662867}; Vmax=8.6 mmol/min/mg enzyme {ECO:0000269|PubMed:4197660}; |
| Metal Binding | |
| Rhea ID | RHEA:17561 |
| Cross Reference Brenda |