Cholinesterase

NameCholinesterase
Synonyms
  • 3.1.1.8
  • Acylcholine acylhydrolase
  • Butyrylcholine esterase
  • CHE1
  • Choline esterase II
  • Pseudocholinesterase
Gene NameBCHE
OrganismHuman
Amino acid sequence
>lcl|BSEQ0016706|Cholinesterase
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
Number of residues602
Molecular Weight68417.575
Theoretical pI7.47
GO Classification
Functions
  • enzyme binding
  • identical protein binding
  • catalytic activity
  • acetylcholinesterase activity
  • beta-amyloid binding
  • choline binding
  • cholinesterase activity
Processes
  • negative regulation of synaptic transmission
  • synaptic transmission
  • choline metabolic process
  • cocaine metabolic process
  • neuroblast differentiation
  • cellular protein metabolic process
  • negative regulation of cell proliferation
  • response to glucocorticoid
  • learning
  • response to folic acid
  • acetylcholine catabolic process
  • response to drug
  • response to alkaloid
Components
  • endoplasmic reticulum lumen
  • blood microparticle
  • nuclear envelope lumen
  • membrane
  • extracellular region
General FunctionIdentical protein binding
Specific FunctionEsterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID1311630
UniProtKB IDP06276
UniProtKB Entry NameCHLE_HUMAN
Cellular LocationSecreted
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
GenBank Gene IDM32391
GeneCard IDNot Available
GenAtlas IDBCHE
HGNC IDHGNC:983
Chromosome Location3
Locus3q26.1-q26.2
References
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  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. 1349196
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  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. 15563885
  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. 15781196
  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. 16788378
  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. 17700357
  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. 18075469
  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. 18300943
  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. 25264279