Cholinesterase

Details

Name
Cholinesterase
Synonyms
  • 3.1.1.8
  • Acylcholine acylhydrolase
  • Butyrylcholine esterase
  • CHE1
  • Choline esterase II
  • Pseudocholinesterase
Gene Name
BCHE
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016706|Cholinesterase
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
Number of residues
602
Molecular Weight
68417.575
Theoretical pI
7.47
GO Classification
Functions
acetylcholinesterase activity / beta-amyloid binding / catalytic activity / choline binding / cholinesterase activity / enzyme binding / identical protein binding
Processes
acetylcholine catabolic process / cellular protein metabolic process / choline metabolic process / cocaine metabolic process / learning / negative regulation of cell proliferation / negative regulation of synaptic transmission / neuroblast differentiation / response to alkaloid / response to drug / response to folic acid / response to glucocorticoid / synaptic transmission
Components
blood microparticle / endoplasmic reticulum lumen / extracellular region / membrane / nuclear envelope lumen
General Function
Identical protein binding
Specific Function
Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0016707|Cholinesterase (BCHE)
ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC
ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA
GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC
TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG
TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT
TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT
TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG
ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT
CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA
TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG
TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA
ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA
AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG
GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC
TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT
CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG
ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT
AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT
GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA
GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT
TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT
GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG
GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA
TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA
AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGGTGGGCA
AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC
TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG
AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG
ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT
TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG
GGTCTCTAA
Chromosome Location
3
Locus
3q26.1-q26.2
External Identifiers
ResourceLink
UniProtKB IDP06276
UniProtKB Entry NameCHLE_HUMAN
GenBank Protein ID1311630
GenBank Gene IDM32391
GenAtlas IDBCHE
HGNC IDHGNC:983
General References
  1. Prody CA, 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. 1987 Jun;84(11):3555-9. [Article]
  2. McTiernan C, Adkins S, Chatonnet A, Vaughan TA, Bartels CF, Kott M, Rosenberry TL, La Du BN, Lockridge O: Brain cDNA clone for human cholinesterase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6682-6. [Article]
  3. Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O: Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry. 1990 Jan 9;29(1):124-31. [Article]
  4. 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL: Complete amino acid sequence of human serum cholinesterase. J Biol Chem. 1987 Jan 15;262(2):549-57. [Article]
  7. Weber A, Butterweck H, Mais-Paul U, Teschner W, Lei L, Muchitsch EM, Kolarich D, Altmann F, Ehrlich HJ, Schwarz HP: Biochemical, molecular and preclinical characterization of a double-virus-reduced human butyrylcholinesterase preparation designed for clinical use. Vox Sang. 2011 Apr;100(3):285-97. doi: 10.1111/j.1423-0410.2010.01415.x. Epub 2010 Oct 15. [Article]
  8. Lockridge O, Adkins S, La Du BN: Location of disulfide bonds within the sequence of human serum cholinesterase. J Biol Chem. 1987 Sep 25;262(27):12945-52. [Article]
  9. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [Article]
  10. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [Article]
  11. Kolarich D, Weber A, Pabst M, Stadlmann J, Teschner W, Ehrlich H, Schwarz HP, Altmann F: Glycoproteomic characterization of butyrylcholinesterase from human plasma. Proteomics. 2008 Jan;8(2):254-63. doi: 10.1002/pmic.200700720. [Article]
  12. Chilukuri N, Duysen EG, Parikh K, diTargiani R, Doctor BP, Lockridge O, Saxena A: Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents. Mol Pharmacol. 2009 Sep;76(3):612-7. doi: 10.1124/mol.109.055665. Epub 2009 Jun 19. [Article]
  13. 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. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  14. Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [Article]
  15. Amitay M, Shurki A: The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger. Proteins. 2009 Nov 1;77(2):370-7. doi: 10.1002/prot.22442. [Article]
  16. Aryal UK, Lin CT, Kim JS, Heibeck TH, Wang J, Qian WJ, Lin Y: Identification of phosphorylated butyrylcholinesterase in human plasma using immunoaffinity purification and mass spectrometry. Anal Chim Acta. 2012 Apr 20;723:68-75. doi: 10.1016/j.aca.2012.02.023. Epub 2012 Feb 19. [Article]
  17. 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. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  18. Delacour H, Lushchekina S, Mabboux I, Bousquet A, Ceppa F, Schopfer LM, 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. 2014 Jul 23;9(7):e101552. doi: 10.1371/journal.pone.0101552. eCollection 2014. [Article]
  19. Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F: Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem. 2003 Oct 17;278(42):41141-7. Epub 2003 Jul 17. [Article]
  20. Nachon F, Asojo OA, Borgstahl GE, 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. 2005 Feb 1;44(4):1154-62. [Article]
  21. Ngamelue MN, Homma K, Lockridge O, Asojo OA: Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):723-7. Epub 2007 Aug 10. [Article]
  22. Frasco MF, Colletier JP, Weik M, Carvalho F, Guilhermino L, Stojan J, Fournier D: Mechanisms of cholinesterase inhibition by inorganic mercury. FEBS J. 2007 Apr;274(7):1849-61. Epub 2007 Mar 12. [Article]
  23. Carletti E, Li H, Li B, Ekstrom F, Nicolet Y, Loiodice M, Gillon E, Froment MT, Lockridge O, Schopfer LM, Masson P, Nachon F: Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation. J Am Chem Soc. 2008 Nov 26;130(47):16011-20. doi: 10.1021/ja804941z. [Article]
  24. Carletti E, Aurbek N, Gillon E, Loiodice M, Nicolet Y, Fontecilla-Camps JC, 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. 2009 Jun 12;421(1):97-106. doi: 10.1042/BJ20090091. [Article]
  25. Nachon F, Carletti E, Ronco C, Trovaslet M, Nicolet Y, Jean L, Renard PY: 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. 2013 Aug 1;453(3):393-9. doi: 10.1042/BJ20130013. [Article]
  26. McGuire MC, Nogueira CP, Bartels CF, Lightstone H, Hajra A, Van der Spek AF, Lockridge O, La Du BN: Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. Proc Natl Acad Sci U S A. 1989 Feb;86(3):953-7. [Article]
  27. Bartels CF, James K, La Du BN: DNA mutations associated with the human butyrylcholinesterase J-variant. Am J Hum Genet. 1992 May;50(5):1104-14. [Article]
  28. Nogueira CP, Bartels CF, McGuire MC, Adkins S, Lubrano T, Rubinstein HM, Lightstone H, Van der Spek AF, Lockridge O, La Du BN: Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase. Am J Hum Genet. 1992 Oct;51(4):821-8. [Article]
  29. 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. 1992 Mar;31(3):357-62. [Article]
  30. Jensen FS, Bartels CF, La Du BN: Structural basis of the butyrylcholinesterase H-variant segregating in two Danish families. Pharmacogenetics. 1992 Oct;2(5):234-40. [Article]
  31. Maekawa M, Sudo K, Kanno T, Kotani K, Dey DC, Ishikawa J, Izumi M, Etoh K: Genetic basis of the silent phenotype of serum butyrylcholinesterase in three compound heterozygotes. Clin Chim Acta. 1995 Feb 28;235(1):41-57. [Article]
  32. 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. 1995;6(4):349-51. [Article]
  33. Primo-Parmo SL, Bartels CF, Wiersema B, van der Spek AF, Innis JW, La Du BN: Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene. Am J Hum Genet. 1996 Jan;58(1):52-64. [Article]
  34. 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. 1997 Nov;61(Pt 6):491-6. [Article]
  35. 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. 1997 Nov 17;240(2):372-5. [Article]
  36. Maekawa M, Sudo K, Dey DC, Ishikawa J, Izumi M, Kotani K, Kanno T: Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan. Clin Chem. 1997 Jun;43(6 Pt 1):924-9. [Article]
  37. Primo-Parmo SL, Lightstone H, La Du BN: Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase. Pharmacogenetics. 1997 Feb;7(1):27-34. [Article]
  38. 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. 1998 Jun 22;274(2):159-66. [Article]
  39. 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. 1999 May;283(1-2):33-42. [Article]
  40. Boeck AT, Fry DL, Sastre A, Lockridge O: Naturally occurring mutation, Asp70his, in human butyrylcholinesterase. Ann Clin Biochem. 2002 Mar;39(Pt 2):154-6. [Article]
  41. Yen T, Nightingale BN, Burns JC, Sullivan DR, Stewart PM: Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population. Clin Chem. 2003 Aug;49(8):1297-308. [Article]
  42. On-Kei Chan A, Lam CW, Tong SF, Man Tung C, Yung K, Chan YW, Au KM, Yuen YP, Hung CT, Ng KP, Shek CC: Novel mutations in the BCHE gene in patients with no butyrylcholinesterase activity. Clin Chim Acta. 2005 Jan;351(1-2):155-9. [Article]
  43. Souza RL, Mikami LR, Maegawa RO, Chautard-Freire-Maia EA: Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample. Mol Genet Metab. 2005 Apr;84(4):349-53. Epub 2005 Jan 24. [Article]
  44. Manoharan I, Wieseler S, Layer PG, Lockridge O, Boopathy R: Naturally occurring mutation Leu307Pro of human butyrylcholinesterase in the Vysya community of India. Pharmacogenet Genomics. 2006 Jul;16(7):461-8. [Article]
  45. Mikami LR, Wieseler S, Souza RL, Schopfer LM, Lockridge O, Chautard-Freire-Maia EA: Expression of three naturally occurring genetic variants (G75R, E90D, I99M) of the BCHE gene of human butyrylcholinesterase. Pharmacogenet Genomics. 2007 Sep;17(9):681-5. [Article]
  46. Gatke MR, Bundgaard JR, 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. 2007 Nov;17(11):995-9. [Article]
  47. Mikami LR, Wieseler S, Souza RL, Schopfer LM, Nachon F, Lockridge O, Chautard-Freire-Maia EA: Five new naturally occurring mutations of the BCHE gene and frequencies of 12 butyrylcholinesterase alleles in a Brazilian population. Pharmacogenet Genomics. 2008 Mar;18(3):213-8. doi: 10.1097/FPC.0b013e3282f5107e. [Article]
  48. Delacour H, Lushchekina S, Mabboux I, Ceppa F, Masson P, Schopfer LM, Lockridge O: Characterization of a novel butyrylcholinesterase point mutation (p.Ala34Val), "silent" with mivacurium. Biochem Pharmacol. 2014 Dec 1;92(3):476-83. doi: 10.1016/j.bcp.2014.09.014. Epub 2014 Sep 28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00772Malathionapproved, investigationalyesinhibitorDetails
DB036729-N-Phenylmethylamino-TacrineexperimentalunknownDetails
DB00122Cholineapproved, nutraceuticalunknownproduct ofDetails
DB00989Rivastigmineapproved, investigationalyesinhibitorDetails
DB00677Isoflurophateapproved, investigational, withdrawnyesinhibitorDetails
DB00941HexafluroniumapprovedyesinhibitorDetails
DB00944DemecariumapprovedunknowninhibitorDetails
DB01057EchothiophateapprovedyesinhibitorDetails
DB02811Diethyl phosphonateexperimentalunknownDetails
DB03568Butyric Acidexperimental, investigationalunknownDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails
DB03822Ethyl dihydrogen phosphateexperimentalunknownDetails
DB04250ButyrylthiocholineexperimentalunknownsubstrateDetails
DB01400Neostigmineapproved, vet_approvedunknowninhibitorDetails
DB00202SuccinylcholineapprovednosubstrateDetails
DB00358Mefloquineapproved, investigationalunknowninhibitorDetails
DB00392ProfenamineapprovedunknowninhibitorDetails
DB00477Chlorpromazineapproved, investigational, vet_approvedunknowninhibitorDetails
DB00527Cinchocaineapproved, vet_approvedunknowninhibitorDetails
DB00871TerbutalineapprovedunknowninhibitorDetails
DB01035ProcainamideapprovedunknowninhibitorDetails
DB01116Trimethaphanapproved, investigationalunknownsubstrateDetails
DB01122AmbenoniumapprovedunknowninhibitorDetails
DB01337PancuroniumapprovedunknowninhibitorDetails
DB01408BambuterolinvestigationalunknownsubstrateinhibitorDetails
DB03568Butyric Acidexperimental, investigationalunknownligandDetails
DB03822Ethyl dihydrogen phosphateexperimentalunknownligandDetails
DB04250ButyrylthiocholineexperimentalunknownsubstrateDetails
DB03976PhosphorylisopropaneexperimentalunknownligandDetails
DB00382Tacrineapproved, investigational, withdrawnyesinhibitorDetails
DB00449DipivefrinapprovedyessubstrateDetails
DB07681DODECANESULFONATE IONexperimentalunknownDetails
DB079409-(3-IODOBENZYLAMINO)-1,2,3,4-TETRAHYDROACRIDINEexperimentalunknownDetails
DB08200(1R)-menthyl hexyl phosphonate groupexperimentalunknownDetails
DB08201(1S)-menthyl hexyl phosphonate groupexperimentalunknownDetails
DB08658Ethyl hydrogen diethylamidophosphateexperimentalunknownDetails
DB02845Methylphosphinic AcidexperimentalunknownDetails
DB02845Methylphosphinic AcidexperimentalunknowninhibitorDetails
DB00545Pyridostigmineapproved, investigationalyesinhibitorDetails
DB00674GalantamineapprovedunknowninhibitorDetails
DB00677Isoflurophateapproved, investigational, withdrawnunknowninhibitorDetails
DB00733Pralidoximeapproved, vet_approvedyesactivatorDetails
DB01010EdrophoniumapprovedyesinhibitorDetails
DB01226MivacuriumapprovedunknownDetails
DB04892PhenserineinvestigationalunknowninhibitorDetails
DB06756Betaineapproved, investigational, nutraceuticalunknowninhibitorDetails
DB06774CapsaicinapprovedunknowninhibitorDetails
DB01161Chloroprocaineapproved, investigationalunknownsubstrateDetails
DB00856Chlorphenesinapproved, experimentalunknowninducerDetails
DB04920Clevidipineapproved, investigationalunknownsubstrateDetails
DB00979CyclopentolateapprovedunknownsubstrateDetails
DB01245DecamethoniumapprovedunknowninhibitorDetails
DB00711Diethylcarbamazineapproved, investigational, vet_approvedunknowninhibitorDetails
DB01135DoxacuriumapprovedunknownsubstrateDetails
DB01364EphedrineapprovedunknownsubstrateDetails
DB00585NizatidineapprovedunknowninhibitorDetails
DB00892Oxybuprocaineapproved, investigationalunknownsubstrateDetails
DB00082PegvisomantapprovedunknowninhibitorDetails
DB00183PentagastrinapprovedunknowninducerDetails
DB00790PerindoprilapprovedunknowninhibitorDetails
DB01338PipecuroniumapprovedunknowninhibitorDetails
DB00515CisplatinapprovedunknowninhibitorDetails
DB00721Procaineapproved, investigational, vet_approvedunknownsubstrateinhibitorDetails
DB00178RamiprilapprovedunknowninhibitorDetails
DB05386RegramostiminvestigationalunknowninhibitorDetails
DB05875Sar9, Met (O2)11-Substance PinvestigationalunknownsubstrateDetails
DB00391Sulpirideapproved, investigationalunknowninhibitorDetails
DB00620Triamcinoloneapproved, vet_approvedunknowninducerDetails
DB00508Triflupromazineapproved, vet_approvedunknowninhibitorDetails
DB08893MirabegronapprovednosubstrateDetails
DB08897AclidiniumapprovednosubstrateDetails
DB00762Irinotecanapproved, investigationalunknownsubstrateDetails
DB11397Dichlorvosvet_approvedunknownDetails
DB09205Moxisylyteapproved, investigationalnosubstrateDetails
DB01221Ketamineapproved, vet_approvedyesinhibitorDetails
DB09288PropacetamolexperimentalnosubstrateDetails
DB14006Choline salicylateapproved, nutraceuticalunknownproduct ofDetails
DB11148Butambenapproved, withdrawnnosubstrateDetails
DB01199TubocurarineapprovednosubstrateDetails
DB06692Aprotininapproved, investigational, withdrawnnoinhibitorDetails
DB04572Thiotepaapproved, investigationalnoinhibitorDetails
DB00888Mechlorethamineapproved, investigationalnoinhibitorDetails
DB14031TretamineexperimentalnoinhibitorDetails
DB00907Cocaineapproved, illicitnosubstrateDetails
DB00843DonepezilapprovedunknowninducerDetails
DB00868BenzonatateapprovednosubstrateDetails
DB00545Pyridostigmineapproved, investigationalnosubstrateDetails
DB01226MivacuriumapprovedunknownsubstrateDetails
DB03128Acetylcholineapproved, investigationalnosubstrateDetails
DB01064Isoprenalineapproved, investigationalnoinhibitorDetails
DB01408BambuterolinvestigationalunknowninhibitorDetails