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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.
25-OCT-2017, entry version 192.
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 BCHE DEFICIENCY 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 ENZYME 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, ENZYME 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 ENZYME 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY CYS-61; SER-65; PHE-153; GLU-198; GLY-226;
THR-229; ARG-499 AND LEU-546, AND CHARACTERIZATION OF VARIANTS BCHE
DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY PRO-335, AND CHARACTERIZATION OF VARIANT BCHE
DEFICIENCY 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
BCHE DEFICIENCY 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 BCHE DEFICIENCY 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 BCHE DEFICIENCY CYS-361, VARIANTS ARG-40; MET-322 AND TRP-498,
CHARACTERIZATION OF VARIANT BCHE DEFICIENCY 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 BCHE DEFICIENCY VAL-62 AND GLY-98, AND CHARACTERIZATION OF
VARIANTS BCHE DEFICIENCY 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: An acylcholine + H(2)O = choline + a
carboxylate. {ECO:0000269|PubMed:19368529,
ECO:0000269|PubMed:19452557}.
-!- ENZYME 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 (BChE deficiency)
[MIM:177400]: A metabolic disorder characterized by prolonged
apnea after the use of certain anesthetic drugs, including the
muscle relaxants succinylcholine or mivacurium and other ester
local anesthetics. 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.
UniGene; Hs.420483; -.
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.
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; -.
ProteinModelPortal; P06276; -.
SMR; P06276; -.
BioGrid; 107064; 40.
DIP; DIP-46476N; -.
IntAct; P06276; 1.
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; -.
iPTMnet; P06276; -.
PhosphoSitePlus; P06276; -.
BioMuta; BCHE; -.
DMDM; 116353; -.
EPD; P06276; -.
MaxQB; P06276; -.
PaxDb; P06276; -.
PeptideAtlas; P06276; -.
PRIDE; P06276; -.
DNASU; 590; -.
Ensembl; ENST00000264381; ENSP00000264381; ENSG00000114200.
GeneID; 590; -.
KEGG; hsa:590; -.
UCSC; uc003fem.5; human.
CTD; 590; -.
DisGeNET; 590; -.
EuPathDB; HostDB:ENSG00000114200.9; -.
GeneCards; BCHE; -.
HGNC; HGNC:983; BCHE.
HPA; HPA001560; -.
MalaCards; BCHE; -.
MIM; 177400; gene+phenotype.
neXtProt; NX_P06276; -.
OpenTargets; ENSG00000114200; -.
Orphanet; 132; Butyrylcholinesterase deficiency.
Orphanet; 413693; Curariform drugs toxicity.
PharmGKB; PA25294; -.
eggNOG; KOG4389; Eukaryota.
eggNOG; COG2272; LUCA.
GeneTree; ENSGT00760000118946; -.
HOVERGEN; HBG008839; -.
InParanoid; P06276; -.
KO; K01050; -.
OMA; GNNAFFY; -.
OrthoDB; EOG091G0I4G; -.
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; -.
CleanEx; HS_BCHE; -.
ExpressionAtlas; P06276; baseline and differential.
Genevisible; P06276; HS.
GO; GO:0072562; C:blood microparticle; IDA: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:0016788; F:hydrolase activity, acting on ester bonds; TAS:Reactome.
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 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:0042493; P:response to drug; 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.
ProDom; PD415333; AChE_tetra; 1.
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 BChE deficiency).
{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 BChE deficiency;
dbSNP:rs56309853).
{ECO:0000269|PubMed:9191541}.
/FTId=VAR_040012.
VARIANT 56 56 F -> I (in BChE deficiency;
dbSNP:rs531738678).
{ECO:0000269|PubMed:12881446}.
/FTId=VAR_040013.
VARIANT 61 61 Y -> C (in BChE deficiency; enzymatically
inactive in the plasma;
dbSNP:rs116097205).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040014.
VARIANT 62 62 A -> V (in BChE deficiency; 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).
{ECO:0000269|PubMed:25264279}.
/FTId=VAR_072730.
VARIANT 65 65 P -> S (in BChE deficiency; seems to
cause reduced expression of the protein;
dbSNP:rs148170012).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040015.
VARIANT 98 98 D -> G (in BChE deficiency; 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 BChE deficiency).
{ECO:0000269|PubMed:11928765}.
/FTId=VAR_040016.
VARIANT 103 103 G -> R (in BChE deficiency; reduced
enzyme activity).
{ECO:0000269|PubMed:15781196,
ECO:0000269|PubMed:17700357}.
/FTId=VAR_072095.
VARIANT 118 118 E -> D (in BChE deficiency; the mutant
undergoes rapid degradation).
{ECO:0000269|PubMed:15781196,
ECO:0000269|PubMed:17700357}.
/FTId=VAR_072096.
VARIANT 124 124 N -> Y (in BChE deficiency).
{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 BChE deficiency;
dbSNP:rs3732880).
{ECO:0000269|PubMed:9191541}.
/FTId=VAR_040018.
VARIANT 143 143 G -> D (in BChE deficiency;
dbSNP:rs201820739).
{ECO:0000269|PubMed:9110359}.
/FTId=VAR_040019.
VARIANT 153 153 L -> F (in BChE deficiency; seems to
cause reduced expression of the protein;
dbSNP:rs747598704).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040020.
VARIANT 156 156 Y -> C (in BChE deficiency;
dbSNP:rs121918558).
{ECO:0000269|PubMed:9543549}.
/FTId=VAR_040021.
VARIANT 170 170 V -> M (in BChE deficiency; allele H
variant; dbSNP:rs527843566).
{ECO:0000269|PubMed:1306123}.
/FTId=VAR_040022.
VARIANT 198 198 D -> E (in BChE deficiency; seems to
cause reduced expression of the protein;
dbSNP:rs781368801).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040023.
VARIANT 226 226 S -> G (in BChE deficiency; enzymatically
inactive in the plasma;
dbSNP:rs370077923).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040024.
VARIANT 227 227 A -> V (in BChE deficiency).
{ECO:0000269|PubMed:9694584}.
/FTId=VAR_040025.
VARIANT 229 229 A -> T (in BChE deficiency; enzymatically
inactive in the plasma).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040026.
VARIANT 232 232 V -> D (in BChE deficiency).
{ECO:0000269|PubMed:25054547}.
/FTId=VAR_072098.
VARIANT 271 271 T -> M (in BChE deficiency; allele
fluoride-1; dbSNP:rs28933389).
{ECO:0000269|PubMed:11928765,
ECO:0000269|PubMed:1415224}.
/FTId=VAR_040027.
VARIANT 278 278 T -> P (in BChE deficiency).
{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 BChE deficiency;
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 BChE deficiency; expressed at
very low level; dbSNP:rs104893684).
{ECO:0000269|PubMed:16788378}.
/FTId=VAR_040031.
VARIANT 356 356 A -> D (in BChE deficiency;
dbSNP:rs770337031).
{ECO:0000269|PubMed:18075469}.
/FTId=VAR_040032.
VARIANT 358 358 L -> I (in BChE deficiency; 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 BChE deficiency; results in
20% of activity compared to wild-type).
{ECO:0000269|PubMed:18300943}.
/FTId=VAR_072100.
VARIANT 393 393 G -> R (in BChE deficiency;
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 BChE deficiency;
dbSNP:rs745364489).
{ECO:0000269|PubMed:12881446,
ECO:0000269|PubMed:15563885}.
/FTId=VAR_040034.
VARIANT 418 418 G -> V (in BChE deficiency; allele
fluoride-2; dbSNP:rs28933390).
{ECO:0000269|PubMed:1415224}.
/FTId=VAR_040035.
VARIANT 446 446 F -> S (in BChE deficiency).
{ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_040036.
VARIANT 488 488 E -> K (in BChE deficiency;
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 BChE deficiency; seems to
cause reduced expression of the protein).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040038.
VARIANT 502 502 F -> L (in BChE deficiency;
dbSNP:rs769316835).
{ECO:0000269|PubMed:15563885}.
/FTId=VAR_040039.
VARIANT 525 525 E -> V (in BChE deficiency; allele J
variant; dbSNP:rs121918556).
{ECO:0000269|PubMed:1349196}.
/FTId=VAR_040040.
VARIANT 543 543 R -> C (in BChE deficiency;
dbSNP:rs199660374).
{ECO:0000269|PubMed:10404729,
ECO:0000269|PubMed:7634491,
ECO:0000269|PubMed:9191541}.
/FTId=VAR_040041.
VARIANT 546 546 Q -> L (in BChE deficiency; seems to
cause reduced expression of the protein).
{ECO:0000269|PubMed:8554068}.
/FTId=VAR_040042.
VARIANT 567 567 A -> T (in BChE deficiency; 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:1P0I}.
STRAND 39 42 {ECO:0000244|PDB:1P0I}.
STRAND 44 48 {ECO:0000244|PDB:1P0I}.
STRAND 51 60 {ECO:0000244|PDB:1P0I}.
HELIX 67 69 {ECO:0000244|PDB:1P0I}.
STRAND 82 85 {ECO:0000244|PDB:1P0I}.
HELIX 105 108 {ECO:0000244|PDB:1P0I}.
STRAND 116 118 {ECO:0000244|PDB:2XMB}.
STRAND 122 130 {ECO:0000244|PDB:1P0I}.
STRAND 133 141 {ECO:0000244|PDB:1P0I}.
TURN 145 147 {ECO:0000244|PDB:1P0I}.
HELIX 154 156 {ECO:0000244|PDB:1P0I}.
HELIX 159 165 {ECO:0000244|PDB:1P0I}.
STRAND 168 172 {ECO:0000244|PDB:1P0I}.
HELIX 177 181 {ECO:0000244|PDB:1P0I}.
STRAND 190 192 {ECO:0000244|PDB:2WSL}.
HELIX 194 209 {ECO:0000244|PDB:1P0I}.
HELIX 210 213 {ECO:0000244|PDB:1P0I}.
STRAND 215 225 {ECO:0000244|PDB:1P0I}.
HELIX 227 237 {ECO:0000244|PDB:1P0I}.
HELIX 239 244 {ECO:0000244|PDB:1P0I}.
STRAND 246 252 {ECO:0000244|PDB:1P0I}.
TURN 258 260 {ECO:0000244|PDB:4BDS}.
HELIX 264 277 {ECO:0000244|PDB:1P0I}.
HELIX 285 292 {ECO:0000244|PDB:1P0I}.
HELIX 297 304 {ECO:0000244|PDB:1P0I}.
HELIX 305 307 {ECO:0000244|PDB:1P0I}.
STRAND 308 310 {ECO:0000244|PDB:1P0I}.
STRAND 324 326 {ECO:0000244|PDB:1P0I}.
HELIX 331 336 {ECO:0000244|PDB:1P0I}.
STRAND 345 350 {ECO:0000244|PDB:1P0I}.
STRAND 352 354 {ECO:0000244|PDB:1P0P}.
HELIX 355 358 {ECO:0000244|PDB:1P0I}.
TURN 359 361 {ECO:0000244|PDB:1P0I}.
STRAND 367 369 {ECO:0000244|PDB:4B0P}.
HELIX 375 385 {ECO:0000244|PDB:1P0I}.
STRAND 387 389 {ECO:0000244|PDB:2WSL}.
HELIX 391 401 {ECO:0000244|PDB:1P0I}.
TURN 405 408 {ECO:0000244|PDB:2WIK}.
HELIX 412 425 {ECO:0000244|PDB:1P0I}.
HELIX 427 438 {ECO:0000244|PDB:1P0I}.
TURN 439 441 {ECO:0000244|PDB:1P0I}.
STRAND 444 449 {ECO:0000244|PDB:1P0I}.
HELIX 460 462 {ECO:0000244|PDB:1P0I}.
TURN 466 469 {ECO:0000244|PDB:1P0I}.
HELIX 470 473 {ECO:0000244|PDB:1P0I}.
HELIX 476 478 {ECO:0000244|PDB:1P0I}.
HELIX 480 482 {ECO:0000244|PDB:2WSL}.
HELIX 486 505 {ECO:0000244|PDB:1P0I}.
TURN 511 514 {ECO:0000244|PDB:1P0I}.
TURN 523 525 {ECO:0000244|PDB:1P0I}.
STRAND 527 531 {ECO:0000244|PDB:1P0I}.
STRAND 538 541 {ECO:0000244|PDB:1P0I}.
HELIX 544 551 {ECO:0000244|PDB:1P0I}.
TURN 552 555 {ECO:0000244|PDB:1P0I}.
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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