| IED ID | IndEnz0005001020 |
| Enzyme Type ID | lipase001020 |
| Protein Name |
Cholinesterase EC 3.1.1.8 Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Pseudocholinesterase |
| Gene Name | BCHE CHE1 |
| 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 | MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL |
| Enzyme Length | 602 |
| Uniprot Accession Number | P06276 |
| Absorption | |
| Active Site | ACT_SITE 226; /note="Acyl-ester intermediate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12869558"; ACT_SITE 353; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:12869558"; ACT_SITE 466; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:12869558" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging. {ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529}. |
| Binding Site | BINDING 110; /note=Tacrine; inhibitor; /evidence=ECO:0007744|PDB:4BDS; BINDING 466; /note=Tacrine; via carbonyl oxygen; inhibitor; /evidence=ECO:0007744|PDB:4BDS |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an acylcholine + H2O = a carboxylate + choline + H(+); Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8; Evidence={ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19452557}; |
| DNA Binding | |
| EC Number | 3.1.1.8 |
| Enzyme Function | FUNCTION: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. {ECO:0000269|PubMed:19452557, ECO:0000269|PubMed:19542320}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (21); Binding site (2); Chain (1); Disulfide bond (4); Glycosylation (10); Helix (26); Modified residue (1); Natural variant (44); Region (1); Signal peptide (1); Turn (8) |
| Keywords | 3D-structure;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Phosphoprotein;Reference proteome;Secreted;Serine esterase;Sialic acid;Signal |
| Interact With | P54252; P46379-2; Itself; P55212; O75190-2; O14901; P13473-2; O75400-2; P62826; P67812 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}. |
| Modified Residue | MOD_RES 226; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:22444575 |
| Post Translational Modification | PTM: N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type. {ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:20946535}. |
| Signal Peptide | SIGNAL 1..28; /evidence="ECO:0000269|PubMed:20946535, ECO:0000269|PubMed:3542989" |
| Structure 3D | Electron microscopy (1); X-ray crystallography (74) |
| Cross Reference PDB | 1P0I; 1P0M; 1P0P; 1P0Q; 1XLU; 1XLV; 1XLW; 2J4C; 2PM8; 2WID; 2WIF; 2WIG; 2WIJ; 2WIK; 2WIL; 2WSL; 2XMB; 2XMC; 2XMD; 2XMG; 2XQF; 2XQG; 2XQI; 2XQJ; 2XQK; 2Y1K; 3DJY; 3DKK; 3O9M; 4AQD; 4AXB; 4B0O; 4B0P; 4BBZ; 4BDS; 4TPK; 4XII; 5DYT; 5DYW; 5DYY; 5K5E; 5LKR; 5NN0; 6EMI; 6EP4; 6EQP; 6EQQ; 6ESJ; 6ESY; 6EUL; 6EYF; 6EZ2; 6F7Q; 6I0B; 6I0C; 6I2T; 6QAA; 6QAB; 6QAC; 6QAD; 6QAE; 6R6V; 6R6W; 6RUA; 6SAM; 6T9P; 6T9S; 6XTA; 6ZWI; 7AIY; 7AMZ; 7AWG; 7AWH; 7AWI; 7BGC; |
| Mapped Pubmed ID | 10430518; 11053835; 11125748; 11436125; 11725818; 11738493; 11749053; 11793025; 11848688; 11849755; 11856322; 11856351; 12009429; 12044901; 12074828; 12130740; 12387584; 12417112; 12668920; 12687586; 12724618; 12811800; 12901493; 14622273; 14686935; 14735258; 15111428; 15256494; 15258737; 15386241; 15449725; 15465921; 15519745; 15690550; 15696543; 15731585; 15802910; 15834019; 15907830; 16020944; 16105444; 16213467; 16278840; 16288482; 16289064; 16298355; 16429499; 16504521; 16731619; 16801396; 16824336; 16909200; 16962996; 16973370; 17192624; 17275003; 17289852; 17318303; 17335779; 17350607; 17410321; 1748670; 17503475; 17660298; 17690023; 17698511; 17701416; 17852836; 17917325; 17923322; 17996334; 18076380; 18165570; 18237553; 18290843; 18322399; 18334913; 18396350; 18422653; 18457821; 18550040; 18555211; 18640242; 18778798; 18780301; 19006190; 19010318; 19019080; 19056482; 19156168; 19217865; 19280057; 19383604; 19474452; 19481150; 19578796; 19617863; 19685167; 19713000; 19913121; 19956635; 20056567; 20058037; 20122907; 20143968; 20193849; 20308990; 20356562; 20379614; 20399202; 20529763; 20538374; 20628086; 20644562; 20677742; 20807286; 20879632; 20883446; 20886866; 21029050; 21091433; 21438623; 21454498; 21473860; 21493754; 21505234; 21530486; 21547979; 21576115; 21862451; 22040426; 22157615; 22294139; 22331678; 22402324; 22560633; 22726956; 22750491; 22778864; 22901043; 22917637; 22922115; 22935510; 23000450; 23022600; 23044488; 23063927; 23123771; 23339663; 23419831; 23466605; 23508960; 23650977; 23689009; 23782236; 24001779; 24041656; 24125115; 24312228; 24399815; 24446003; 24473115; 24479631; 24870023; 24951323; 25179377; 25226236; 25336127; 25447891; 25471831; 25835709; 26116179; 26189613; 26223693; 26439437; 26496610; 26497592; 26757188; 26955768; 27031121; 27062896; 27106529; 27109752; 27405689; 27468571; 27551784; 27567841; 27908752; 27911294; 28000737; 28225154; 28465191; 28544359; 28698452; 29077024; 29177431; 29186056; 29227101; 29254094; 29358722; 29393817; 29631548; 30031971; 30061034; 30093245; 30385318; 30410011; 30538207; 30707402; 30851693; 30864579; 30914707; 31071335; 31914836; 32006676; 32250307; 32380361; 32639532; 32705955; 32859055; 32919297; 32998065; 33024248; 33375115; 33617373; 33672269; 33829779; 33838585; 34299650; 34530376; 6777177; 6838677; 9536100; 9682830; 9836756; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,418 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.0 uM for butyrylthiocholine (at 25 degrees Celsius) {ECO:0000269|PubMed:25054547}; |
| Metal Binding | |
| Rhea ID | RHEA:21964 |
| Cross Reference Brenda | 3.1.1.8; |