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Cholinesterase (EC 3.1.1.8) (Acylcholine acylhydrolase) (Butyrylcholine esterase) (Choline esterase II) (Pseudocholinesterase)

 CHLE_HUMAN              Reviewed;         602 AA.
P06276; A8K7P8;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
31-JUL-2019, entry version 208.
RecName: Full=Cholinesterase;
EC=3.1.1.8;
AltName: Full=Acylcholine acylhydrolase;
AltName: Full=Butyrylcholine esterase;
AltName: Full=Choline esterase II;
AltName: Full=Pseudocholinesterase;
Flags: Precursor;
Name=BCHE; Synonyms=CHE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetus;
PubMed=3035536; DOI=10.1073/pnas.84.11.3555;
Prody C.A., Zevin-Sonkin D., Gnatt A., Goldberg O., Soreq H.;
"Isolation and characterization of full-length cDNA clones coding for
cholinesterase from fetal human tissues.";
Proc. Natl. Acad. Sci. U.S.A. 84:3555-3559(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3477799; DOI=10.1073/pnas.84.19.6682;
McTiernan C., Adkins S., Chatonnet A., Vaughan T.A., Bartels C.F.,
Kott M., Rosenberry T.L., la Du B.N., Lockridge O.;
"Brain cDNA clone for human cholinesterase.";
Proc. Natl. Acad. Sci. U.S.A. 84:6682-6686(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2322535; DOI=10.1021/bi00453a015;
Arpagaus M., Kott M., Vatsis K.P., Bartels C.F., la Du B.N.,
Lockridge O.;
"Structure of the gene for human butyrylcholinesterase. Evidence for a
single copy.";
Biochemistry 29:124-131(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-567.
TISSUE=Stomach;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 29-602, AND SIGNAL SEQUENCE CLEAVAGE SITE.
TISSUE=Plasma;
PubMed=3542989;
Lockridge O., Bartels C.F., Vaughan T.A., Wong C.K., Norton S.E.,
Johnson L.L.;
"Complete amino acid sequence of human serum cholinesterase.";
J. Biol. Chem. 262:549-557(1987).
[7]
PROTEIN SEQUENCE OF 29-37; 43-68; 71-163; 167-290; 294-522; 528-543
AND 549-602, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, AND
HOMOTETRAMERIZATION.
TISSUE=Plasma;
PubMed=20946535; DOI=10.1111/j.1423-0410.2010.01415.x;
Weber A., Butterweck H., Mais-Paul U., Teschner W., Lei L.,
Muchitsch E.M., Kolarich D., Altmann F., Ehrlich H.J., Schwarz H.P.;
"Biochemical, molecular and preclinical characterization of a double-
virus-reduced human butyrylcholinesterase preparation designed for
clinical use.";
Vox Sang. 100:285-297(2011).
[8]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=3115973;
Lockridge O., Adkins S., la Du B.N.;
"Location of disulfide bonds within the sequence of human serum
cholinesterase.";
J. Biol. Chem. 262:12945-12952(1987).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369;
ASN-483; ASN-509 AND ASN-514.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
GLYCOSYLATION AT ASN-45; ASN-85; ASN-134; ASN-269; ASN-284; ASN-369
AND ASN-483, AND CHARACTERIZATION OF GLYCOSYLATION.
PubMed=18203274; DOI=10.1002/pmic.200700720;
Kolarich D., Weber A., Pabst M., Stadlmann J., Teschner W.,
Ehrlich H., Schwarz H.P., Altmann F.;
"Glycoproteomic characterization of butyrylcholinesterase from human
plasma.";
Proteomics 8:254-263(2008).
[12]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
PubMed=19542320; DOI=10.1124/mol.109.055665;
Chilukuri N., Duysen E.G., Parikh K., diTargiani R., Doctor B.P.,
Lockridge O., Saxena A.;
"Adenovirus-transduced human butyrylcholinesterase in mouse blood
functions as a bioscavenger of chemical warfare nerve agents.";
Mol. Pharmacol. 76:612-617(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
GLYCOSYLATION AT ASN-284.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[15]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=19452557; DOI=10.1002/prot.22442;
Amitay M., Shurki A.;
"The structure of G117H mutant of butyrylcholinesterase: nerve agents
scavenger.";
Proteins 77:370-377(2009).
[16]
PHOSPHORYLATION AT SER-226.
PubMed=22444575; DOI=10.1016/j.aca.2012.02.023;
Aryal U.K., Lin C.T., Kim J.S., Heibeck T.H., Wang J., Qian W.J.,
Lin Y.;
"Identification of phosphorylated butyrylcholinesterase in human
plasma using immunoaffinity purification and mass spectrometry.";
Anal. Chim. Acta 723:68-75(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT BCHED ASP-232.
PubMed=25054547; DOI=10.1371/journal.pone.0101552;
Delacour H., Lushchekina S., Mabboux I., Bousquet A., Ceppa F.,
Schopfer L.M., Lockridge O., Masson P.;
"Characterization of a novel BCHE 'silent' allele: point mutation
(p.Val204Asp) causes loss of activity and prolonged apnea with
suxamethonium.";
PLoS ONE 9:E101552-E101552(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH
SUBSTRATE, SUBUNIT, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369
AND ASN-513, DISULFIDE BONDS, AND ACTIVE SITE.
PubMed=12869558; DOI=10.1074/jbc.M210241200;
Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., Nachon F.;
"Crystal structure of human butyrylcholinesterase and of its complexes
with substrate and products.";
J. Biol. Chem. 278:41141-41147(2003).
[20]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH
ECHOTHIOPHATE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-85; ASN-134;
ASN-269; ASN-369 AND ASN-513.
PubMed=15667209; DOI=10.1021/bi048238d;
Nachon F., Asojo O.A., Borgstahl G.E.O., Masson P., Lockridge O.;
"Role of water in aging of human butyrylcholinesterase inhibited by
echothiophate: the crystal structure suggests two alternative
mechanisms of aging.";
Biochemistry 44:1154-1162(2005).
[21]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION
AT ASN-85; ASN-134; ASN-369 AND ASN-513, AND SUBUNIT.
PubMed=17768338; DOI=10.1107/S1744309107037335;
Ngamelue M.N., Homma K., Lockridge O., Asojo O.A.;
"Crystallization and X-ray structure of full-length recombinant human
butyrylcholinesterase.";
Acta Crystallogr. F 63:723-727(2007).
[22]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITH
MERCURY IONS AND BUTANOIC ACID, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, AND ACTIVITY
REGULATION.
PubMed=17355286; DOI=10.1111/j.1742-4658.2007.05732.x;
Frasco M.F., Colletier J.-P., Weik M., Carvalho F., Guilhermino L.,
Stojan J., Fournier D.;
"Mechanisms of cholinesterase inhibition by inorganic mercury.";
FEBS J. 274:1849-1861(2007).
[23]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH
TABUN, ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
GLYCOSYLATION AT ASN-85; ASN-134; ASN-284; ASN-369 AND ASN-513.
PubMed=18975951; DOI=10.1021/ja804941z;
Carletti E., Li H., Li B., Ekstroem F., Nicolet Y., Loiodice M.,
Gillon E., Froment M.T., Lockridge O., Schopfer L.M., Masson P.,
Nachon F.;
"Aging of cholinesterases phosphylated by tabun proceeds through O-
dealkylation.";
J. Am. Chem. Soc. 130:16011-16020(2008).
[24]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN
ANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND
ASN-513, AND ACTIVITY REGULATION.
PubMed=19368529; DOI=10.1042/BJ20090091;
Carletti E., Aurbek N., Gillon E., Loiodice M., Nicolet Y.,
Fontecilla-Camps J.C., Masson P., Thiermann H., Nachon F., Worek F.;
"Structure-activity analysis of aging and reactivation of human
butyrylcholinesterase inhibited by analogues of tabun.";
Biochem. J. 421:97-106(2009).
[25]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH
TACRINE, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-85; ASN-134;
ASN-269; ASN-284; ASN-369 AND ASN-513.
PubMed=23679855; DOI=10.1042/BJ20130013;
Nachon F., Carletti E., Ronco C., Trovaslet M., Nicolet Y., Jean L.,
Renard P.Y.;
"Crystal structures of human cholinesterases in complex with huprine W
and tacrine: elements of specificity for anti-Alzheimer's drugs
targeting acetyl- and butyryl-cholinesterase.";
Biochem. J. 453:393-399(2013).
[26]
VARIANT BCHED GLY-98.
PubMed=2915989; DOI=10.1073/pnas.86.3.953;
McGuire M.C., Nogueira C.P., Bartels C.F., Lightstone H., Hajra A.,
van der Spek A.F.L., Lockridge O., la Du B.N.;
"Identification of the structural mutation responsible for the
dibucaine-resistant (atypical) variant form of human serum
cholinesterase.";
Proc. Natl. Acad. Sci. U.S.A. 86:953-957(1989).
[27]
VARIANT BCHED VAL-525.
PubMed=1349196;
Bartels C.F., James K., La Du B.N.;
"DNA mutations associated with the human butyrylcholinesterase J-
variant.";
Am. J. Hum. Genet. 50:1104-1114(1992).
[28]
VARIANTS BCHED MET-271 AND VAL-418.
PubMed=1415224;
Nogueira C.P., Bartels C.F., McGuire M.C., Adkins S., Lubrano T.,
Rubinstein H.M., Lightstone H., Van Der Spek A.F.L., Lockridge O.,
La Du B.N.;
"Identification of two different point mutations associated with the
fluoride-resistant phenotype for human butyrylcholinesterase.";
Am. J. Hum. Genet. 51:821-828(1992).
[29]
VARIANT BCHED ARG-393.
PubMed=1611188;
Hada T., Muratani K., Ohue T., Imanishi H., Moriwaki Y., Itoh M.,
Amuro Y., Higashino K.;
"A variant serum cholinesterase and a confirmed point mutation at Gly-
365 to Arg found in a patient with liver cirrhosis.";
Intern. Med. 31:357-362(1992).
[30]
VARIANTS BCHED GLY-98 AND MET-170.
PubMed=1306123;
Jensen F.S., Bartels C.F., La Du B.N.;
"Structural basis of the butyrylcholinesterase H-variant segregating
in two Danish families.";
Pharmacogenetics 2:234-240(1992).
[31]
VARIANTS BCHED PRO-278; ARG-393; SER-446; CYS-543 AND THR-567.
PubMed=7634491; DOI=10.1016/0009-8981(95)06014-1;
Maekawa M., Sudo K., Kanno T., Kotani K., Dey D.C., Ishikawa J.,
Izumi M., Etoh K.;
"Genetic basis of the silent phenotype of serum butyrylcholinesterase
in three compound heterozygotes.";
Clin. Chim. Acta 235:41-57(1995).
[32]
VARIANT BCHED ILE-358.
PubMed=8680411; DOI=10.1002/humu.1380060411;
Iida S., Kinoshita M., Fujii H., Moriyama Y., Nakamura Y., Yura N.,
Moriwaki K.;
"Mutations of human butyrylcholinesterase gene in a family with
hypocholinesterasemia.";
Hum. Mutat. 6:349-351(1995).
[33]
VARIANTS BCHED CYS-61; SER-65; PHE-153; GLU-198; GLY-226; THR-229;
ARG-499 AND LEU-546, AND CHARACTERIZATION OF VARIANTS BCHED SER-65;
PHE-153; GLU-198; ARG-499 AND LEU-546.
PubMed=8554068;
Primo-Parmo S.L., Bartels C.F., Wiersema B., van der Spek A.F.L.,
Innis J.W., La Du B.N.;
"Characterization of 12 silent alleles of the human
butyrylcholinesterase (BCHE) gene.";
Am. J. Hum. Genet. 58:52-64(1996).
[34]
VARIANT BCHED CYS-156.
PubMed=9543549; DOI=10.1017/S0003480097006520;
Hidaka K., Iuchi I., Tomita M., Watanabe Y., Minatogawa Y.,
Iwasaki K., Gotoh K., Shimizu C.;
"Genetic analysis of a Japanese patient with butyrylcholinesterase
deficiency.";
Ann. Hum. Genet. 61:491-496(1997).
[35]
VARIANT BUTYRYLCHOLINESTERASE DEFICIENCY ILE-358.
PubMed=9388484; DOI=10.1006/bbrc.1997.7658;
Sudo K., Maekawa M., Akizuki S., Magara T., Ogasawara H., Tanaka T.;
"Human butyrylcholinesterase L330I mutation belongs to a fluoride-
resistant gene, by expression in human fetal kidney cells.";
Biochem. Biophys. Res. Commun. 240:372-375(1997).
[36]
VARIANTS BCHED ILE-32 DEL; MET-52; SER-128; PRO-278; ARG-295; ILE-358;
ARG-393; SER-446; CYS-543 AND THR-567.
PubMed=9191541;
Maekawa M., Sudo K., Dey D.C., Ishikawa J., Izumi M., Kotani K.,
Kanno T.;
"Genetic mutations of butyrylcholine esterase identified from
phenotypic abnormalities in Japan.";
Clin. Chem. 43:924-929(1997).
[37]
VARIANTS BCHED GLY-98 AND ASP-143.
PubMed=9110359;
Primo-Parmo S.L., Lightstone H., La Du B.N.;
"Characterization of an unstable variant (BChE115D) of human
butyrylcholinesterase.";
Pharmacogenetics 7:27-34(1997).
[38]
VARIANT BCHED VAL-227.
PubMed=9694584; DOI=10.1016/S0009-8981(98)00058-8;
Sakamoto N., Hidaka K., Fujisawa T., Maeda M., Iuchi I.;
"Identification of a point mutation associated with a silent phenotype
of human serum butyrylcholinesterase - a case of familial
cholinesterasemia.";
Clin. Chim. Acta 274:159-166(1998).
[39]
VARIANTS BCHED ILE-358; ARG-393 AND CYS-543.
PubMed=10404729; DOI=10.1016/S0009-8981(99)00030-3;
Asanuma K., Yagihashi A., Uehara N., Kida T., Watanabe N.;
"Three point mutations of human butyrylcholinesterase in a Japanese
family and the alterations of three-dimensional structure.";
Clin. Chim. Acta 283:33-42(1999).
[40]
VARIANTS BCHED GLY-98; HIS-98; MET-271 AND THR-567.
PubMed=11928765; DOI=10.1258/0004563021901775;
Boeck A.T., Fry D.L., Sastre A., Lockridge O.;
"Naturally occurring mutation, Asp70His, in human
butyrylcholinesterase.";
Ann. Clin. Biochem. 39:154-156(2002).
[41]
VARIANTS BCHED ILE-56; TYR-124; CYS-414 AND LYS-488.
PubMed=12881446; DOI=10.1373/49.8.1297;
Yen T., Nightingale B.N., Burns J.C., Sullivan D.R., Stewart P.M.;
"Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine
apnea in an Australian population.";
Clin. Chem. 49:1297-1308(2003).
[42]
VARIANTS BCHED CYS-414 AND LEU-502.
PubMed=15563885; DOI=10.1016/j.cccn.2004.09.004;
On-Kei Chan A., Lam C.-W., Tong S.-F., Man Tung C., Yung K.,
Chan Y.-W., Au K.-M., Yuen Y.-P., Hung C.-T., Ng K.-P., Shek C.-C.;
"Novel mutations in the BCHE gene in patients with no
butyrylcholinesterase activity.";
Clin. Chim. Acta 351:155-159(2005).
[43]
VARIANT MET-127, AND VARIANTS BCHED GLY-98; ARG-103 AND ASP-118.
PubMed=15781196; DOI=10.1016/j.ymgme.2004.12.005;
Souza R.L., Mikami L.R., Maegawa R.O., Chautard-Freire-Maia E.A.;
"Four new mutations in the BCHE gene of human butyrylcholinesterase in
a Brazilian blood donor sample.";
Mol. Genet. Metab. 84:349-353(2005).
[44]
VARIANT BCHED PRO-335, AND CHARACTERIZATION OF VARIANT BCHED PRO-335.
PubMed=16788378; DOI=10.1097/01.fpc.0000197464.37211.77;
Manoharan I., Wieseler S., Layer P.G., Lockridge O., Boopathy R.;
"Naturally occurring mutation Leu307Pro of human butyrylcholinesterase
in the Vysya community of India.";
Pharmacogenet. Genomics 16:461-468(2006).
[45]
CHARACTERIZATION OF VARIANT MET-127, AND CHARACTERIZATION OF VARIANTS
BCHED ARG-103 AND ASP-118.
PubMed=17700357; DOI=10.1097/01.fpc.0000236333.49422.86;
Mikami L.R., Wieseler S., Souza R.L., Schopfer L.M., Lockridge O.,
Chautard-Freire-Maia E.A.;
"Expression of three naturally occurring genetic variants (G75R, E90D,
I99M) of the BCHE gene of human butyrylcholinesterase.";
Pharmacogenet. Genomics 17:681-685(2007).
[46]
VARIANT BCHED ASP-356.
PubMed=18075469; DOI=10.1097/FPC.0b013e3282f06646;
Gaetke M.R., Bundgaard J.R., Viby-Mogensen J.;
"Two novel mutations in the BCHE gene in patients with prolonged
duration of action of mivacurium or succinylcholine during
anaesthesia.";
Pharmacogenet. Genomics 17:995-999(2007).
[47]
VARIANT BCHED CYS-361, VARIANTS ARG-40; MET-322 AND TRP-498,
CHARACTERIZATION OF VARIANT BCHED CYS-361, AND CHARACTERIZATION OF
VARIANTS ARG-40; MET-322 AND TRP-498.
PubMed=18300943; DOI=10.1097/FPC.0b013e3282f5107e;
Mikami L.R., Wieseler S., Souza R.L., Schopfer L.M., Nachon F.,
Lockridge O., Chautard-Freire-Maia E.A.;
"Five new naturally occurring mutations of the BCHE gene and
frequencies of 12 butyrylcholinesterase alleles in a Brazilian
population.";
Pharmacogenet. Genomics 18:213-218(2008).
[48]
VARIANTS BCHED VAL-62 AND GLY-98, AND CHARACTERIZATION OF VARIANTS
BCHED VAL-62 AND GLY-98.
PubMed=25264279; DOI=10.1016/j.bcp.2014.09.014;
Delacour H., Lushchekina S., Mabboux I., Ceppa F., Masson P.,
Schopfer L.M., Lockridge O.;
"Characterization of a novel butyrylcholinesterase point mutation
(p.Ala34Val), 'silent' with mivacurium.";
Biochem. Pharmacol. 92:476-483(2014).
-!- 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}.
-!- 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};
-!- 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}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=18.0 uM for butyrylthiocholine (at 25 degrees Celsius)
{ECO:0000269|PubMed:25054547};
-!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers.
{ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209,
ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338,
ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:19542320, ECO:0000269|PubMed:3115973}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-7936069, EBI-7936069;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:19542320}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
Present in most cells except erythrocytes.
{ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}.
-!- 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}.
-!- DISEASE: Butyrylcholinesterase deficiency (BCHED) [MIM:617936]: An
autosomal recessive metabolic condition characterized by increased
sensitivity to certain anesthetic drugs, including the muscle
relaxants succinylcholine or mivacurium. BCHED results in slower
hydrolysis of these drugs and, consequently, a prolonged
neuromuscular block, leading to apnea. The duration of the
prolonged apnea varies significantly depending on the extent of
the enzyme deficiency. {ECO:0000269|PubMed:10404729,
ECO:0000269|PubMed:11928765, ECO:0000269|PubMed:12881446,
ECO:0000269|PubMed:1306123, ECO:0000269|PubMed:1349196,
ECO:0000269|PubMed:1415224, ECO:0000269|PubMed:15563885,
ECO:0000269|PubMed:15781196, ECO:0000269|PubMed:1611188,
ECO:0000269|PubMed:16788378, ECO:0000269|PubMed:17700357,
ECO:0000269|PubMed:18075469, ECO:0000269|PubMed:18300943,
ECO:0000269|PubMed:25054547, ECO:0000269|PubMed:25264279,
ECO:0000269|PubMed:2915989, ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:8554068, ECO:0000269|PubMed:8680411,
ECO:0000269|PubMed:9110359, ECO:0000269|PubMed:9191541,
ECO:0000269|PubMed:9388484, ECO:0000269|PubMed:9543549,
ECO:0000269|PubMed:9694584}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M32391; AAA99296.1; -; Genomic_DNA.
EMBL; M32389; AAA99296.1; JOINED; Genomic_DNA.
EMBL; M32390; AAA99296.1; JOINED; Genomic_DNA.
EMBL; M16541; AAA98113.1; -; mRNA.
EMBL; M16474; AAA52015.1; -; mRNA.
EMBL; AK292063; BAF84752.1; -; mRNA.
EMBL; BC018141; AAH18141.1; -; mRNA.
CCDS; CCDS3198.1; -.
PIR; A33769; ACHU.
RefSeq; NP_000046.1; NM_000055.3.
PDB; 1EHO; Model; -; A=30-560.
PDB; 1EHQ; Model; -; A=30-560.
PDB; 1KCJ; Model; -; A=30-560.
PDB; 1P0I; X-ray; 2.00 A; A=29-557.
PDB; 1P0M; X-ray; 2.38 A; A=29-557.
PDB; 1P0P; X-ray; 2.30 A; A=29-557.
PDB; 1P0Q; X-ray; 2.43 A; A=29-557.
PDB; 1XLU; X-ray; 2.20 A; A=29-557.
PDB; 1XLV; X-ray; 2.25 A; A=29-557.
PDB; 1XLW; X-ray; 2.10 A; A=29-557.
PDB; 2J4C; X-ray; 2.75 A; A=29-557.
PDB; 2PM8; X-ray; 2.80 A; A/B=29-602.
PDB; 2WID; X-ray; 2.30 A; A=29-557.
PDB; 2WIF; X-ray; 2.25 A; A=29-557.
PDB; 2WIG; X-ray; 2.15 A; A=29-557.
PDB; 2WIJ; X-ray; 2.10 A; A=29-557.
PDB; 2WIK; X-ray; 2.10 A; A=29-557.
PDB; 2WIL; X-ray; 3.10 A; A/B=29-557.
PDB; 2WSL; X-ray; 2.00 A; A=29-557.
PDB; 2XMB; X-ray; 2.10 A; A=29-557.
PDB; 2XMC; X-ray; 2.40 A; A=29-557.
PDB; 2XMD; X-ray; 2.30 A; A=29-557.
PDB; 2XMG; X-ray; 2.70 A; A=29-557.
PDB; 2XQF; X-ray; 2.10 A; A=31-557.
PDB; 2XQG; X-ray; 2.30 A; A=31-557.
PDB; 2XQI; X-ray; 2.60 A; A=31-557.
PDB; 2XQJ; X-ray; 2.40 A; A=31-557.
PDB; 2XQK; X-ray; 2.40 A; A=31-557.
PDB; 2Y1K; X-ray; 2.50 A; A=29-557.
PDB; 3DJY; X-ray; 2.10 A; A=29-557.
PDB; 3DKK; X-ray; 2.31 A; A=29-557.
PDB; 3O9M; X-ray; 2.98 A; A/B=29-602.
PDB; 4AQD; X-ray; 2.50 A; A/B=29-557.
PDB; 4AXB; X-ray; 2.40 A; A=31-557.
PDB; 4B0O; X-ray; 2.35 A; A=29-557.
PDB; 4B0P; X-ray; 2.50 A; A=29-557.
PDB; 4BBZ; X-ray; 2.70 A; A=29-557.
PDB; 4BDS; X-ray; 2.10 A; A=29-557.
PDB; 4TPK; X-ray; 2.70 A; A/B=1-602.
PDB; 4XII; X-ray; 2.70 A; A/B=29-572.
PDB; 5DYT; X-ray; 2.55 A; A/B=28-557.
PDB; 5DYW; X-ray; 2.50 A; A/B=28-557.
PDB; 5DYY; X-ray; 2.65 A; A/B=28-557.
PDB; 5K5E; X-ray; 2.80 A; A/B=29-557.
PDB; 5LKR; X-ray; 2.52 A; A/B=29-602.
PDB; 5NN0; X-ray; 2.10 A; A=29-557.
PDB; 6EMI; X-ray; 2.48 A; A/B=29-557.
PDB; 6EP4; X-ray; 2.30 A; A=29-557.
PDB; 6EQP; X-ray; 2.35 A; A=29-557.
PDB; 6EQQ; X-ray; 2.40 A; A=29-557.
PDB; 6ESJ; X-ray; 2.98 A; A/B=29-557.
PDB; 6ESY; X-ray; 2.80 A; A/B=29-557.
PDB; 6EUL; X-ray; 2.60 A; A=31-558.
PDB; 6EYF; X-ray; 2.60 A; A=31-557.
PDB; 6EZ2; X-ray; 2.70 A; A/B=31-557.
PDB; 6F7Q; X-ray; 2.60 A; A/B=29-557.
PDB; 6I0B; X-ray; 2.38 A; A=29-557.
PDB; 6I0C; X-ray; 2.67 A; A=29-557.
PDB; 6I2T; EM; 5.70 A; A/B/C/D=29-602.
PDB; 6QAA; X-ray; 1.90 A; A=1-557.
PDB; 6QAB; X-ray; 2.49 A; A=1-557.
PDB; 6QAC; X-ray; 2.77 A; A=1-557.
PDB; 6QAD; X-ray; 2.50 A; A=1-557.
PDB; 6QAE; X-ray; 2.49 A; A=1-557.
PDBsum; 1EHO; -.
PDBsum; 1EHQ; -.
PDBsum; 1KCJ; -.
PDBsum; 1P0I; -.
PDBsum; 1P0M; -.
PDBsum; 1P0P; -.
PDBsum; 1P0Q; -.
PDBsum; 1XLU; -.
PDBsum; 1XLV; -.
PDBsum; 1XLW; -.
PDBsum; 2J4C; -.
PDBsum; 2PM8; -.
PDBsum; 2WID; -.
PDBsum; 2WIF; -.
PDBsum; 2WIG; -.
PDBsum; 2WIJ; -.
PDBsum; 2WIK; -.
PDBsum; 2WIL; -.
PDBsum; 2WSL; -.
PDBsum; 2XMB; -.
PDBsum; 2XMC; -.
PDBsum; 2XMD; -.
PDBsum; 2XMG; -.
PDBsum; 2XQF; -.
PDBsum; 2XQG; -.
PDBsum; 2XQI; -.
PDBsum; 2XQJ; -.
PDBsum; 2XQK; -.
PDBsum; 2Y1K; -.
PDBsum; 3DJY; -.
PDBsum; 3DKK; -.
PDBsum; 3O9M; -.
PDBsum; 4AQD; -.
PDBsum; 4AXB; -.
PDBsum; 4B0O; -.
PDBsum; 4B0P; -.
PDBsum; 4BBZ; -.
PDBsum; 4BDS; -.
PDBsum; 4TPK; -.
PDBsum; 4XII; -.
PDBsum; 5DYT; -.
PDBsum; 5DYW; -.
PDBsum; 5DYY; -.
PDBsum; 5K5E; -.
PDBsum; 5LKR; -.
PDBsum; 5NN0; -.
PDBsum; 6EMI; -.
PDBsum; 6EP4; -.
PDBsum; 6EQP; -.
PDBsum; 6EQQ; -.
PDBsum; 6ESJ; -.
PDBsum; 6ESY; -.
PDBsum; 6EUL; -.
PDBsum; 6EYF; -.
PDBsum; 6EZ2; -.
PDBsum; 6F7Q; -.
PDBsum; 6I0B; -.
PDBsum; 6I0C; -.
PDBsum; 6I2T; -.
PDBsum; 6QAA; -.
PDBsum; 6QAB; -.
PDBsum; 6QAC; -.
PDBsum; 6QAD; -.
PDBsum; 6QAE; -.
SMR; P06276; -.
BioGrid; 107064; 40.
DIP; DIP-46476N; -.
IntAct; P06276; 1.
MINT; P06276; -.
STRING; 9606.ENSP00000264381; -.
BindingDB; P06276; -.
ChEMBL; CHEMBL1914; -.
DrugBank; DB08200; (1R)-MENTHYL HEXYL PHOSPHONATE GROUP.
DrugBank; DB08201; (1S)-MENTHYL HEXYL PHOSPHONATE GROUP.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB03672; 9-N-Phenylmethylamino-Tacrine.
DrugBank; DB08897; Aclidinium.
DrugBank; DB01122; Ambenonium.
DrugBank; DB01408; Bambuterol.
DrugBank; DB03568; Butyric Acid.
DrugBank; DB04250; Butyrylthiocholine.
DrugBank; DB06774; Capsaicin.
DrugBank; DB01161; Chloroprocaine.
DrugBank; DB00856; Chlorphenesin.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB00122; Choline.
DrugBank; DB00527; Cinchocaine.
DrugBank; DB00515; Cisplatin.
DrugBank; DB04920; Clevidipine.
DrugBank; DB00979; Cyclopentolate.
DrugBank; DB01245; Decamethonium.
DrugBank; DB00944; Demecarium.
DrugBank; DB00711; Diethylcarbamazine.
DrugBank; DB02811; Diethylphosphono Group.
DrugBank; DB00449; Dipivefrin.
DrugBank; DB07681; DODECANESULFONATE ION.
DrugBank; DB01135; Doxacurium chloride.
DrugBank; DB01395; Drospirenone.
DrugBank; DB01525; Ecgonine.
DrugBank; DB01057; Echothiophate.
DrugBank; DB01010; Edrophonium.
DrugBank; DB01364; Ephedrine.
DrugBank; DB00392; Ethopropazine.
DrugBank; DB03822; Ethyl Dihydrogen Phosphate.
DrugBank; DB08658; ETHYL HYDROGEN DIETHYLAMIDOPHOSPHATE.
DrugBank; DB00674; Galantamine.
DrugBank; DB06756; Glycine betaine.
DrugBank; DB00941; Hexafluronium.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00677; Isoflurophate.
DrugBank; DB00772; Malathion.
DrugBank; DB00358; Mefloquine.
DrugBank; DB02845; Methylphosphinic Acid.
DrugBank; DB08893; Mirabegron.
DrugBank; DB01226; Mivacurium.
DrugBank; DB04251; Monoisopropyl Ester Phosphonic Acid Group.
DrugBank; DB01400; Neostigmine.
DrugBank; DB00585; Nizatidine.
DrugBank; DB00892; Oxybuprocaine.
DrugBank; DB01337; Pancuronium.
DrugBank; DB00082; Pegvisomant.
DrugBank; DB00183; Pentagastrin.
DrugBank; DB00790; Perindopril.
DrugBank; DB04892; Phenserine.
DrugBank; DB01338; Pipecuronium.
DrugBank; DB00733; Pralidoxime.
DrugBank; DB01035; Procainamide.
DrugBank; DB00721; Procaine.
DrugBank; DB00545; Pyridostigmine.
DrugBank; DB00178; Ramipril.
DrugBank; DB05386; recombinant human GM-CSF.
DrugBank; DB00989; Rivastigmine.
DrugBank; DB05875; substance P.
DrugBank; DB00202; Succinylcholine.
DrugBank; DB00391; Sulpiride.
DrugBank; DB00382; Tacrine.
DrugBank; DB00871; Terbutaline.
DrugBank; DB00620; Triamcinolone.
DrugBank; DB00508; Triflupromazine.
DrugBank; DB01116; Trimethaphan.
GuidetoPHARMACOLOGY; 2471; -.
ESTHER; human-BCHE; BCHE.
MEROPS; S09.980; -.
GlyConnect; 1109; -.
iPTMnet; P06276; -.
PhosphoSitePlus; P06276; -.
BioMuta; BCHE; -.
DMDM; 116353; -.
CPTAC; non-CPTAC-2645; -.
EPD; P06276; -.
jPOST; P06276; -.
MaxQB; P06276; -.
PaxDb; P06276; -.
PeptideAtlas; P06276; -.
PRIDE; P06276; -.
ProteomicsDB; 51880; -.
ABCD; P06276; -.
DNASU; 590; -.
Ensembl; ENST00000264381; ENSP00000264381; ENSG00000114200.
GeneID; 590; -.
KEGG; hsa:590; -.
UCSC; uc003fem.5; human.
CTD; 590; -.
DisGeNET; 590; -.
GeneCards; BCHE; -.
HGNC; HGNC:983; BCHE.
HPA; HPA001560; -.
MalaCards; BCHE; -.
MIM; 177400; gene.
MIM; 617936; phenotype.
neXtProt; NX_P06276; -.
OpenTargets; ENSG00000114200; -.
Orphanet; 132; Butyrylcholinesterase deficiency.
Orphanet; 413693; Curariform drugs toxicity.
PharmGKB; PA25294; -.
eggNOG; KOG4389; Eukaryota.
eggNOG; COG2272; LUCA.
GeneTree; ENSGT00940000157023; -.
InParanoid; P06276; -.
KO; K01050; -.
OMA; FPGSEMW; -.
OrthoDB; 1226324at2759; -.
PhylomeDB; P06276; -.
TreeFam; TF315470; -.
BRENDA; 3.1.1.8; 2681.
Reactome; R-HSA-112311; Neurotransmitter clearance.
Reactome; R-HSA-1483191; Synthesis of PC.
Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
SABIO-RK; P06276; -.
SIGNOR; P06276; -.
ChiTaRS; BCHE; human.
EvolutionaryTrace; P06276; -.
GeneWiki; Butyrylcholinesterase; -.
GenomeRNAi; 590; -.
PRO; PR:P06276; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114200; Expressed in 182 organ(s), highest expression level in parietal pleura.
ExpressionAtlas; P06276; baseline and differential.
Genevisible; P06276; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; NAS:UniProtKB.
GO; GO:0003824; F:catalytic activity; NAS:UniProtKB.
GO; GO:0033265; F:choline binding; IEA:Ensembl.
GO; GO:0004104; F:cholinesterase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019695; P:choline metabolic process; IEA:Ensembl.
GO; GO:0050783; P:cocaine metabolic process; TAS:UniProtKB.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
GO; GO:0014016; P:neuroblast differentiation; IEA:Ensembl.
GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR014788; AChE_tetra.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
InterPro; IPR000997; Cholinesterase.
Pfam; PF08674; AChE_tetra; 1.
Pfam; PF00135; COesterase; 1.
PRINTS; PR00878; CHOLNESTRASE.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Hydrolase;
Phosphoprotein; Polymorphism; Reference proteome; Secreted;
Serine esterase; Sialic acid; Signal.
SIGNAL 1 28 {ECO:0000269|PubMed:20946535,
ECO:0000269|PubMed:3542989}.
CHAIN 29 602 Cholinesterase.
/FTId=PRO_0000008613.
REGION 144 145 Substrate binding.
ACT_SITE 226 226 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039,
ECO:0000269|PubMed:12869558}.
ACT_SITE 353 353 Charge relay system.
{ECO:0000269|PubMed:12869558}.
ACT_SITE 466 466 Charge relay system.
{ECO:0000269|PubMed:12869558}.
BINDING 110 110 Tacrine. {ECO:0000244|PDB:4BDS}.
BINDING 466 466 Tacrine; via carbonyl oxygen.
{ECO:0000244|PDB:4BDS}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000269|PubMed:22444575}.
CARBOHYD 45 45 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18203274}.
CARBOHYD 85 85 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12869558,
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:19368529,
ECO:0000269|PubMed:23679855}.
CARBOHYD 134 134 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12869558,
ECO:0000269|PubMed:15667209,
ECO:0000269|PubMed:17355286,
ECO:0000269|PubMed:17768338,
ECO:0000269|PubMed:18203274,
ECO:0000269|PubMed:18975951,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:23679855}.
CARBOHYD 269 269 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12869558,
ECO:0000269|PubMed:15667209,
ECO:0000269|PubMed:17355286,
ECO:0000269|PubMed:18203274,
ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:23679855}.
CARBOHYD 284 284 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:18203274,
ECO:0000269|PubMed:18975951,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:23679855}.
CARBOHYD 369 369 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12869558,
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:19368529,
ECO:0000269|PubMed:23679855}.
CARBOHYD 483 483 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18203274}.
CARBOHYD 509 509 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:3542989}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12869558,
ECO:0000269|PubMed:15667209,
ECO:0000269|PubMed:17355286,
ECO:0000269|PubMed:17768338,
ECO:0000269|PubMed:18975951,
ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:23679855}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:3542989}.
DISULFID 93 120
DISULFID 280 291
DISULFID 428 547
DISULFID 599 599 Interchain.
VARIANT 32 32 Missing (in BCHED).
{ECO:0000269|PubMed:9191541}.
/FTId=VAR_040011.
VARIANT 40 40 K -> R (rare polymorphism; does not
affect enzymatic activity;
dbSNP:rs116047990).
{ECO:0000269|PubMed:18300943}.
/FTId=VAR_072094.
VARIANT 52 52 T -> M (in BCHED; dbSNP:rs56309853).
{ECO:0000269|PubMed:9191541}.
/FTId=VAR_040012.
VARIANT 56 56 F -> I (in BCHED; dbSNP:rs531738678).
{ECO:0000269|PubMed:12881446}.
/FTId=VAR_040013.
VARIANT 61 61 Y -> C (in BCHED; enzymatically inactive
in the plasma; dbSNP:rs116097205).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040014.
VARIANT 62 62 A -> V (in BCHED; reduced enzyme activity
with butyrylthiocholine as substrate;
inactive with butyrylthiocholine as
substrate in the presence of G-98; 2-fold
lower affinity for butyrylthiocholine;
10-fold lower affinity for
butyrylthiocholine in the presence of G-
98; dbSNP:rs1553778274).
{ECO:0000269|PubMed:25264279}.
/FTId=VAR_072730.
VARIANT 65 65 P -> S (in BCHED; seems to cause reduced
expression of the protein;
dbSNP:rs148170012).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040015.
VARIANT 98 98 D -> G (in BCHED; atypical form; reduced
enzyme activity with butyrylthiocholine
as substrate; inactive with
butyrylthiocholine as substrate in the
presence of V-62; 2-fold lower affinity
for butyrylthiocholine; 10-fold lower
affinity for butyrylthiocholine in the
presence of V-62 or at homozygosity;
dbSNP:rs1799807).
{ECO:0000269|PubMed:11928765,
ECO:0000269|PubMed:1306123,
ECO:0000269|PubMed:15781196,
ECO:0000269|PubMed:25264279,
ECO:0000269|PubMed:2915989,
ECO:0000269|PubMed:9110359}.
/FTId=VAR_002360.
VARIANT 98 98 D -> H (in BCHED).
{ECO:0000269|PubMed:11928765}.
/FTId=VAR_040016.
VARIANT 103 103 G -> R (in BCHED; reduced enzyme
activity; dbSNP:rs979653503).
{ECO:0000269|PubMed:15781196,
ECO:0000269|PubMed:17700357}.
/FTId=VAR_072095.
VARIANT 118 118 E -> D (in BCHED; the mutant undergoes
rapid degradation).
{ECO:0000269|PubMed:15781196,
ECO:0000269|PubMed:17700357}.
/FTId=VAR_072096.
VARIANT 124 124 N -> Y (in BCHED; dbSNP:rs1339128583).
{ECO:0000269|PubMed:12881446}.
/FTId=VAR_040017.
VARIANT 127 127 I -> M (rare polymorphism; does not
affect enzyme activity;
dbSNP:rs755600722).
{ECO:0000269|PubMed:15781196,
ECO:0000269|PubMed:17700357}.
/FTId=VAR_072097.
VARIANT 128 128 P -> S (in BCHED; dbSNP:rs3732880).
{ECO:0000269|PubMed:9191541}.
/FTId=VAR_040018.
VARIANT 143 143 G -> D (in BCHED; dbSNP:rs201820739).
{ECO:0000269|PubMed:9110359}.
/FTId=VAR_040019.
VARIANT 153 153 L -> F (in BCHED; seems to cause reduced
expression of the protein;
dbSNP:rs747598704).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040020.
VARIANT 156 156 Y -> C (in BCHED; dbSNP:rs121918558).
{ECO:0000269|PubMed:9543549}.
/FTId=VAR_040021.
VARIANT 170 170 V -> M (in BCHED; allele H variant;
dbSNP:rs527843566).
{ECO:0000269|PubMed:1306123}.
/FTId=VAR_040022.
VARIANT 198 198 D -> E (in BCHED; seems to cause reduced
expression of the protein;
dbSNP:rs781368801).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040023.
VARIANT 226 226 S -> G (in BCHED; enzymatically inactive
in the plasma; dbSNP:rs370077923).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040024.
VARIANT 227 227 A -> V (in BCHED).
{ECO:0000269|PubMed:9694584}.
/FTId=VAR_040025.
VARIANT 229 229 A -> T (in BCHED; enzymatically inactive
in the plasma).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040026.
VARIANT 232 232 V -> D (in BCHED).
{ECO:0000269|PubMed:25054547}.
/FTId=VAR_072098.
VARIANT 271 271 T -> M (in BCHED; allele fluoride-1;
dbSNP:rs28933389).
{ECO:0000269|PubMed:11928765,
ECO:0000269|PubMed:1415224}.
/FTId=VAR_040027.
VARIANT 278 278 T -> P (in BCHED; dbSNP:rs892642457).
{ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_040028.
VARIANT 283 283 E -> D (in dbSNP:rs16849700).
/FTId=VAR_040029.
VARIANT 295 295 K -> R (in BCHED; dbSNP:rs115624085).
{ECO:0000269|PubMed:9191541}.
/FTId=VAR_040030.
VARIANT 322 322 V -> M (rare polymorphism; does not
affect enzymatic activity;
dbSNP:rs754644618).
{ECO:0000269|PubMed:18300943}.
/FTId=VAR_072099.
VARIANT 335 335 L -> P (in BCHED; expressed at very low
level; dbSNP:rs104893684).
{ECO:0000269|PubMed:16788378}.
/FTId=VAR_040031.
VARIANT 356 356 A -> D (in BCHED; dbSNP:rs770337031).
{ECO:0000269|PubMed:18075469}.
/FTId=VAR_040032.
VARIANT 358 358 L -> I (in BCHED; BChE variant form;
fluoride-resistant; dbSNP:rs121918557).
{ECO:0000269|PubMed:10404729,
ECO:0000269|PubMed:8680411,
ECO:0000269|PubMed:9191541,
ECO:0000269|PubMed:9388484}.
/FTId=VAR_002362.
VARIANT 361 361 G -> C (in BCHED; results in 20% of
activity compared to wild-type).
{ECO:0000269|PubMed:18300943}.
/FTId=VAR_072100.
VARIANT 393 393 G -> R (in BCHED; dbSNP:rs115129687).
{ECO:0000269|PubMed:10404729,
ECO:0000269|PubMed:1611188,
ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_040033.
VARIANT 414 414 R -> C (in BCHED; dbSNP:rs745364489).
{ECO:0000269|PubMed:12881446,
ECO:0000269|PubMed:15563885}.
/FTId=VAR_040034.
VARIANT 418 418 G -> V (in BCHED; allele fluoride-2;
dbSNP:rs28933390).
{ECO:0000269|PubMed:1415224}.
/FTId=VAR_040035.
VARIANT 446 446 F -> S (in BCHED).
{ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_040036.
VARIANT 488 488 E -> K (in BCHED; dbSNP:rs200998515).
{ECO:0000269|PubMed:12881446}.
/FTId=VAR_040037.
VARIANT 498 498 R -> W (rare polymorphism; does not
affect enzymatic activity;
dbSNP:rs115017300).
{ECO:0000269|PubMed:18300943}.
/FTId=VAR_072101.
VARIANT 499 499 W -> R (in BCHED; seems to cause reduced
expression of the protein).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040038.
VARIANT 502 502 F -> L (in BCHED; dbSNP:rs769316835).
{ECO:0000269|PubMed:15563885}.
/FTId=VAR_040039.
VARIANT 525 525 E -> V (in BCHED; allele J variant;
dbSNP:rs121918556).
{ECO:0000269|PubMed:1349196}.
/FTId=VAR_040040.
VARIANT 543 543 R -> C (in BCHED; dbSNP:rs199660374).
{ECO:0000269|PubMed:10404729,
ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_040041.
VARIANT 546 546 Q -> L (in BCHED; seems to cause reduced
expression of the protein).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040042.
VARIANT 567 567 A -> T (in BCHED; allele K variant; with
reduced enzyme activity;
dbSNP:rs1803274).
{ECO:0000269|PubMed:11928765,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_002364.
STRAND 33 36 {ECO:0000244|PDB:6QAA}.
STRAND 39 42 {ECO:0000244|PDB:6QAA}.
STRAND 44 48 {ECO:0000244|PDB:6QAA}.
STRAND 51 60 {ECO:0000244|PDB:6QAA}.
HELIX 67 69 {ECO:0000244|PDB:6QAA}.
STRAND 82 85 {ECO:0000244|PDB:6QAA}.
HELIX 105 108 {ECO:0000244|PDB:6QAA}.
STRAND 116 118 {ECO:0000244|PDB:2XMB}.
STRAND 122 130 {ECO:0000244|PDB:6QAA}.
STRAND 133 141 {ECO:0000244|PDB:6QAA}.
TURN 145 147 {ECO:0000244|PDB:6QAA}.
HELIX 154 156 {ECO:0000244|PDB:6QAA}.
HELIX 159 165 {ECO:0000244|PDB:6QAA}.
STRAND 168 172 {ECO:0000244|PDB:6QAA}.
HELIX 177 181 {ECO:0000244|PDB:6QAA}.
STRAND 190 192 {ECO:0000244|PDB:6QAA}.
HELIX 194 209 {ECO:0000244|PDB:6QAA}.
HELIX 210 213 {ECO:0000244|PDB:6QAA}.
STRAND 215 225 {ECO:0000244|PDB:6QAA}.
HELIX 227 237 {ECO:0000244|PDB:6QAA}.
HELIX 239 244 {ECO:0000244|PDB:6QAA}.
STRAND 246 252 {ECO:0000244|PDB:6QAA}.
TURN 258 260 {ECO:0000244|PDB:4BDS}.
HELIX 264 277 {ECO:0000244|PDB:6QAA}.
HELIX 285 292 {ECO:0000244|PDB:6QAA}.
HELIX 297 303 {ECO:0000244|PDB:6QAA}.
HELIX 304 307 {ECO:0000244|PDB:6QAA}.
STRAND 308 310 {ECO:0000244|PDB:6QAA}.
STRAND 324 326 {ECO:0000244|PDB:6QAA}.
HELIX 331 336 {ECO:0000244|PDB:6QAA}.
STRAND 345 350 {ECO:0000244|PDB:6QAA}.
STRAND 352 354 {ECO:0000244|PDB:1P0P}.
HELIX 355 358 {ECO:0000244|PDB:6QAA}.
TURN 359 361 {ECO:0000244|PDB:6QAA}.
STRAND 367 369 {ECO:0000244|PDB:6EQP}.
HELIX 375 385 {ECO:0000244|PDB:6QAA}.
STRAND 387 389 {ECO:0000244|PDB:2WSL}.
HELIX 391 401 {ECO:0000244|PDB:6QAA}.
TURN 405 408 {ECO:0000244|PDB:2WIK}.
HELIX 412 425 {ECO:0000244|PDB:6QAA}.
HELIX 427 438 {ECO:0000244|PDB:6QAA}.
TURN 439 441 {ECO:0000244|PDB:6QAA}.
STRAND 444 449 {ECO:0000244|PDB:6QAA}.
HELIX 460 462 {ECO:0000244|PDB:6QAA}.
TURN 466 469 {ECO:0000244|PDB:6QAA}.
HELIX 470 473 {ECO:0000244|PDB:6QAA}.
HELIX 476 478 {ECO:0000244|PDB:6QAA}.
HELIX 480 482 {ECO:0000244|PDB:6QAA}.
HELIX 486 505 {ECO:0000244|PDB:6QAA}.
TURN 511 514 {ECO:0000244|PDB:6QAA}.
TURN 523 525 {ECO:0000244|PDB:6QAA}.
STRAND 527 531 {ECO:0000244|PDB:6QAA}.
STRAND 538 541 {ECO:0000244|PDB:6QAA}.
HELIX 544 552 {ECO:0000244|PDB:6QAA}.
HELIX 554 556 {ECO:0000244|PDB:6QAA}.
SEQUENCE 602 AA; 68418 MW; C9836409D9057F27 CRC64;
MHSKVTIICI RFLFWFLLLC MLIGKSHTED DIIIATKNGK VRGMNLTVFG GTVTAFLGIP
YAQPPLGRLR FKKPQSLTKW SDIWNATKYA NSCCQNIDQS FPGFHGSEMW NPNTDLSEDC
LYLNVWIPAP KPKNATVLIW IYGGGFQTGT SSLHVYDGKF LARVERVIVV SMNYRVGALG
FLALPGNPEA PGNMGLFDQQ LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPG
SHSLFTRAIL QSGSFNAPWA VTSLYEARNR TLNLAKLTGC SRENETEIIK CLRNKDPQEI
LLNEAFVVPY GTPLSVNFGP TVDGDFLTDM PDILLELGQF KKTQILVGVN KDEGTAFLVY
GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH YTDWVDDQRP ENYREALGDV
VGDYNFICPA LEFTKKFSEW GNNAFFYYFE HRSSKLPWPE WMGVMHGYEI EFVFGLPLER
RDNYTKAEEI LSRSIVKRWA NFAKYGNPNE TQNNSTSWPV FKSTEQKYLT LNTESTRIMT
KLRAQQCRFW TSFFPKVLEM TGNIDEAEWE WKAGFHRWNN YMMDWKNQFN DYTSKKESCV
GL


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[BCHE CHE1] Cholinesterase (EC 3.1.1.8) (Acylcholine acylhydrolase) (Butyrylcholine esterase) (Choline esterase II) (Pseudocholinesterase)
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[axeA TM_0077] Cephalosporin-C deacetylase (EC 3.1.1.41) (Acetylxylan esterase) (EC 3.1.1.72)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BvCmsSIP082_02402 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFB45_10990 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX32_14605 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[celE Cthe_0797] Cellulase/esterase CelE (CtCel5C-CE2) [Includes: Cellulase E (EC 3.2.1.4) (CtCel5C) (Endo-1,4-beta-glucanase E) (EGE) (Endoglucanase E); Acetylxylan esterase / glucomannan deacetylase (EC 3.1.1.-) (EC 3.1.1.72) (CtCE2)]
[CES1 CES2 SES1] Liver carboxylesterase 1 (Acyl-coenzyme A:cholesterol acyltransferase) (ACAT) (Brain carboxylesterase hBr1) (Carboxylesterase 1) (CE-1) (hCE-1) (EC 3.1.1.1) (Cocaine carboxylesterase) (Egasyn) (HMSE) (Methylumbelliferyl-acetate deacetylase 1) (EC 3.1.1.56) (Monocyte/macrophage serine esterase) (Retinyl ester hydrolase) (REH) (Serine esterase 1) (Triacylglycerol hydrolase) (TGH)
[NTE1 YML059C YM9958.03C] Lysophospholipase NTE1 (EC 3.1.1.5) (Intracellular phospholipase B) (Neuropathy target esterase homolog)
[xyn10D-fae1A PRU_2728 ORF02827] Endo-1,4-beta-xylanase/feruloyl esterase [Includes: Endo-1,4-beta-xylanase (EC 3.2.1.8); Feruloyl esterase (EC 3.1.1.73) (Ferulic acid esterase)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[Ces1d Ces3] Carboxylesterase 1D (Carboxyesterase ES-10) (Carboxylesterase 3) (EC 3.1.1.1) (EC 3.1.1.67) (ES-HVEL) (Fatty acid ethyl ester synthase) (FAEE synthase) (Liver carboxylesterase 10) (pI 6.1 esterase)
[SFGH At2g41530 T32G6.5] S-formylglutathione hydrolase (AtSFGH) (EC 3.1.2.12) (Esterase D)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BvCmsC61A_00149 BvCmsH15A_00510 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E5M00_18610 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EPS71_23885 FORC82_1921 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[D14 D88 HTD2 Os03g0203200 LOC_Os03g10620] Strigolactone esterase D14 (EC 3.1.-.-) (Protein DWARF 14) (Protein DWARF 88) (Protein HIGH-TILLERING DWARF 2)
[ESM1 At3g14210 MAG2.6] GDSL esterase/lipase ESM1 (EC 3.1.1.-) (Extracellular lipase ESM1) (Protein EPITHIOSPECIFIER MODIFIER 1) (AtESM1)
[xynS20E] Bifunctional acetylxylan esterase/xylanase XynS20E [Includes: Acetylxylan esterase (EC 3.1.1.72); Endo-1,4-beta-xylanase (Xylanase) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase)]
[hchA DTL90_24035 EL75_1660 EL79_1701 EL80_1732 EO241_11065 EXX06_23780 EXX55_23825 EXX87_24225 NCTC9119_02170 SAMEA3485101_04398] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[PNPLA6 NTE] Neuropathy target esterase (EC 3.1.1.5) (Patatin-like phospholipase domain-containing protein 6)
[aes ybaC b0476 JW0465] Acetyl esterase (EC 3.1.1.-) (EcE)
[Pnpla7] Patatin-like phospholipase domain-containing protein 7 (EC 3.1.1.-) (Neuropathy target esterase-related esterase) (NRE) (NTE-related esterase)
[TGL1 YKL140W YKL5] Sterol esterase TGL1 (EC 3.1.1.13) (Triglyceride lipase-cholesterol esterase 1)
[C1S] Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[D14 At3g03990 T11I18.10] Strigolactone esterase D14 (EC 3.1.-.-) (Protein DWARF 14) (AtD14)
[hchA A8M42_01610 AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC007_02422 ExPECSC065_02714 HmCmsJML122_02218 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[cip2 TRIREDRAFT_123940] 4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.-) (Glucuronoyl esterase) (GE)
[hmpA hmp A8C65_03855 A9R57_17040 ACN002_2592 ACN77_09545 ACN81_26320 ACU57_10360 ACU90_01485 AM270_07210 AM464_04560 AML07_10430 APZ14_05505 AUQ13_13215 AUS26_21665 AW106_11070 BANRA_01097 BANRA_03418 BANRA_04525 BB545_05760 BHS81_15570 BHS87_14445 BJJ90_06510 BK292_20760 BMT53_22940 BMT91_09730 BN17_18391 BUE81_08005 BvCms12BK_01774 BvCms2454_04468 BvCmsA75A_03906 BvCmsF63A_00221 BvCmsH15A_03414 BvCmsHHP001_04806 BvCmsHHP019_04806 BvCmsHHP056_01828 BvCmsJ76A_01917 BvCmsKKP021_02293 BvCmsKSNP019_02755 BvCmsKSP026_04305 BvCmsKSP036_03573 BvCmsKSP039_02804 BvCmsKSP040_04059 BvCmsNSNP006_04915 BvCmsNSNP027_00836 BvCmsNSP045_00359 BvCmsNSP052_02125 BvCmsNSP072_00267 BvCmsOUP014_02948 BvCmsSINP012_04518 BvCmsSINP036_03882 BvCmsSIP010_04889 BvCmsSIP019_03821 BvCmsSIP044_05092 BvCmsSIP082_04619 BVL39_14050 BW690_11150 BZL31_13550 C2U48_21325 C4J69_10505 C5N07_10115 C5P01_05560 C5P43_25010 C6986_16510 C7235_06805 C9E25_16695 COD30_01045 COD46_11500 CRM83_27495 CWS33_10010 D2184_18725 D2185_06690 D3821_11445 D3O91_03570 D3Y67_23905 D9H68_00985 D9I11_00135 D9I18_09865 D9I97_07905 D9J11_04290 D9J44_00060 D9K48_25840 DB357_04025 DIV22_11300 DL545_07245 DL800_19195 DNQ41_17925 DP277_03620 DTL43_01910 E2855_03303 E2863_03210 E5M00_07265 EAI42_06330 EAI44_09410 EC1094V2_1116 EC3234A_44c01590 EC95NR1_01777 ECTO6_01279 ED600_07770 EEP23_02350 EFB45_07490 EFV07_14910 EFV08_03440 EKI52_21980 EPS71_00750 EPS97_09565 EPT01_18845 ERS085365_01518 ERS085374_00038 ERS085416_03760 ERS139211_00868 ERS150873_01392 ERS150876_00857 EXX32_00195 EXX39_12780 EXX71_04790 EXX78_07615 EYD11_06210 EYY78_04395 FORC28_1400 FORC82_1263 HmCms184_00603 HmCmsJML079_04829 HW43_17160 NCTC11022_02631 NCTC11181_03552 NCTC13148_02382 NCTC8500_01411 NCTC8960_04037 NCTC8985_06124 NCTC9036_01390 NCTC9037_01459 NCTC9058_00631 NCTC9062_01812 NCTC9073_04581 NCTC9706_04593 NCTC9962_00729 PU06_05410 RG28_09110 RK56_022045 SAMEA3472043_01058 SAMEA3472044_03009 SAMEA3472070_00042 SAMEA3472080_01630 SAMEA3484427_00463 SAMEA3484429_00572 SAMEA3752553_02327 SAMEA3752557_00946 SAMEA3753097_02775 SK85_02808 WQ89_05840] Flavohemoprotein (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)

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