| IED ID | IndEnz0005001090 |
| Enzyme Type ID | lipase001090 |
| Protein Name |
Acetylcholinesterase AChE EC 3.1.1.7 |
| Gene Name | ACHE |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL |
| Enzyme Length | 614 |
| Uniprot Accession Number | P22303 |
| Absorption | |
| Active Site | ACT_SITE 234; /note=Acyl-ester intermediate; ACT_SITE 365; /note=Charge relay system; ACT_SITE 478; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | BINDING 117; /note=Galanthamine; /evidence=ECO:0007744|PDB:4EY6; BINDING 117; /note=Huperzine A; /evidence=ECO:0007744|PDB:4EY5; BINDING 153; /note=Huprine W; via amide nitrogen; /evidence=ECO:0007744|PDB:4BDT; BINDING 164; /note=Huperzine A; /evidence=ECO:0007744|PDB:4EY5; BINDING 234; /note=Huprine W; /evidence=ECO:0007744|PDB:4BDT; BINDING 368; /note=Galanthamine; /evidence=ECO:0007744|PDB:4EY6; BINDING 368; /note=Huperzine A; /evidence=ECO:0007744|PDB:4EY5; BINDING 470; /note=Huprine W; /evidence=ECO:0007744|PDB:4BDT; BINDING 478; /note=Huprine W; via carbonyl oxygen; /evidence=ECO:0007744|PDB:4BDT |
| 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:1517212};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562; Evidence={ECO:0000305|PubMed:1517212}; |
| DNA Binding | |
| EC Number | 3.1.1.7 |
| Enzyme Function | FUNCTION: Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis. {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1517212, ECO:0000269|PubMed:1748670, ECO:0000269|PubMed:2714437}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (4); Beta strand (24); Binding site (9); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (27); Lipidation (1); Mutagenesis (6); Natural variant (4); Region (1); Sequence conflict (4); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Alternative splicing;Blood group antigen;Cell junction;Cell membrane;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Neurotransmitter degradation;Nucleus;Reference proteome;Secreted;Serine esterase;Signal;Synapse |
| Interact With | Q9Y215; P06733; P63244 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1748670}. Secreted {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform T]: Nucleus. Note=Only observed in apoptotic nuclei.; SUBCELLULAR LOCATION: [Isoform H]: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (64) |
| Cross Reference PDB | 1B41; 1F8U; 1VZJ; 2X8B; 3LII; 4BDT; 4EY4; 4EY5; 4EY6; 4EY7; 4EY8; 4M0E; 4M0F; 4PQE; 5FOQ; 5FPQ; 5HF5; 5HF6; 5HF8; 5HF9; 5HFA; 6CQT; 6CQU; 6CQV; 6CQW; 6CQX; 6CQY; 6CQZ; 6F25; 6NEA; 6NTG; 6NTH; 6NTK; 6NTL; 6NTM; 6NTN; 6NTO; 6O4W; 6O4X; 6O50; 6O52; 6O5R; 6O5S; 6O5V; 6O66; 6O69; 6U34; 6U37; 6U3P; 6WUV; 6WUY; 6WUZ; 6WV1; 6WVC; 6WVO; 6WVP; 6WVQ; 6ZWE; 7D9O; 7D9P; 7D9Q; 7RB5; 7RB6; 7RB7; |
| Mapped Pubmed ID | 10814709; 11105732; 15256494; 15715671; 15974920; 17289852; 18194455; 18396350; 18457821; 19280057; 19730683; 20138030; 20195357; 20883446; 23597562; 24900610; 26751405; 27140636; 27191504; 30462502; 30993792; 31097996; 31132435; 31138650; 31176713; 32019865; 33538594; 33570950; 33672269; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,796 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17561; RHEA:17562 |
| Cross Reference Brenda | 3.1.1.7;3.5.1.13; |