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Identification
HMDB Protein ID HMDBP00525
Secondary Accession Numbers
  • 5774
Name Cholinesterase
Synonyms
  1. Acylcholine acylhydrolase
  2. Butyrylcholine esterase
  3. Choline esterase II
  4. Pseudocholinesterase
Gene Name BCHE
Protein Type Enzyme
Biological Properties
General Function Involved in carboxylesterase activity
Specific Function Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
Pathways
  • Heroin Action Pathway
  • Heroin Metabolism Pathway
  • Irinotecan Action Pathway
  • Irinotecan Metabolism Pathway
Reactions
An acylcholine + Water → Choline + a carboxylate details
GO Classification
Biological Process
response to folic acid
choline metabolic process
response to drug
response to glucocorticoid stimulus
learning
cocaine metabolic process
negative regulation of synaptic transmission
response to alkaloid
synaptic transmission, cholinergic
Cellular Component
endoplasmic reticulum lumen
extracellular space
nuclear envelope lumen
membrane
Component
membrane
cell part
Function
cholinesterase activity
hydrolase activity, acting on ester bonds
catalytic activity
hydrolase activity
carboxylesterase activity
Molecular Function
acetylcholinesterase activity
beta-amyloid binding
carboxylesterase activity
choline binding
enzyme binding
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location 3
Locus 3q26.1-q26.2
SNPs BCHE
Gene Sequence
>1809 bp
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
Protein Properties
Number of Residues 602
Molecular Weight 68417.575
Theoretical pI 7.421
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Cholinesterase
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
GenBank ID Protein 180484
UniProtKB/Swiss-Prot ID P06276
UniProtKB/Swiss-Prot Entry Name CHLE_HUMAN
PDB IDs
GenBank Gene ID M16541
GeneCard ID BCHE
GenAtlas ID BCHE
HGNC ID HGNC:983
References
General References
  1. 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. [PubMed:19159218 ]
  2. 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. [PubMed:14702039 ]
  3. 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. [PubMed:15489334 ]
  4. 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. [PubMed:16335952 ]
  5. 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. [PubMed:14760718 ]
  6. 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. [PubMed:2322535 ]
  7. 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. [PubMed:3035536 ]
  8. 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. [PubMed:3477799 ]
  9. 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. [PubMed:3542989 ]
  10. 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. [PubMed:3115973 ]
  11. 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. [PubMed:19542320 ]
  12. 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. [PubMed:19452557 ]
  13. 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. [PubMed:12869558 ]
  14. 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. [PubMed:15667209 ]
  15. 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. [PubMed:17768338 ]
  16. 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. [PubMed:17355286 ]
  17. 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. [PubMed:18975951 ]
  18. 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. [PubMed:19368529 ]
  19. 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. [PubMed:2915989 ]
  20. 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. [PubMed:1349196 ]
  21. 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. [PubMed:1415224 ]
  22. 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. [PubMed:1611188 ]
  23. 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. [PubMed:1306123 ]
  24. 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. [PubMed:7634491 ]
  25. 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. [PubMed:8680411 ]
  26. 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. [PubMed:8554068 ]
  27. 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. [PubMed:9543549 ]
  28. 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. [PubMed:9388484 ]
  29. 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. [PubMed:9191541 ]
  30. Primo-Parmo SL, Lightstone H, La Du BN: Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase. Pharmacogenetics. 1997 Feb;7(1):27-34. [PubMed:9110359 ]
  31. 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. [PubMed:9694584 ]
  32. 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. [PubMed:10404729 ]
  33. 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. [PubMed:11928765 ]
  34. 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. [PubMed:12881446 ]
  35. 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. [PubMed:15563885 ]
  36. 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. [PubMed:16788378 ]
  37. 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. [PubMed:18075469 ]