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BCHE/Butyrylcholinesterase Protein, Antibody, ELISA Kit, cDNA Clone

BCHE/Butyrylcholinesterase Related Areas

BCHE/Butyrylcholinesterase Related Pathways

BCHE/Butyrylcholinesterase Related Product

    BCHE/Butyrylcholinesterase Summary & Protein Information

    BCHE/Butyrylcholinesterase Background

    Gene Summary: Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage. [provided by RefSeq, Jul 2008]
    General information above from NCBI
    Catalytic activity: An acylcholine + H(2)O = choline + a carboxylate.
    Enzyme regulation: Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging.
    Subunit structure: Homotetramer; disulfide-linked. Dimer of dimers.
    Subcellular location: Secreted.
    Tissue specificity: Detected in blood plasma (at protein level). Present in most cells except erythrocytes.
    Involvement in disease: Butyrylcholinesterase deficiency (BChE deficiency) [MIM:177400]: 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. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Belongs to the type-B carboxylesterase/lipase family.C
    General information above from UniProt

    Butyrylcholinesterase (BCHE), also known as cholinesterase or BuChE, is an enzyme defined as "pseudo" or "non-neuronal" cholinesterase. Butyrylcholinesterase (BCHE) is widely distributed in the nervous system as well as blood plasma. It is constitutively similar to the neuronal acetylcholinesterase, and is a non-specific cholinesterase which hydrolyses many different choline esters. Butyrylcholinesterase (BCHE) is a glycoprotein of 4 identical subunits, that were arranged as a dimer of dimers with each dimer composed of two identical subunits joined by interchain disulfide bonds. Butyrylcholinesterase (BCHE) behaves principally similar to the true enzyme and thus can play a similar role in nerve conduction, although it participates probably only in relatively slow conductive processes and could be involved in other nervous system functions and in neurodegenerative diseases. It can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Purified human serum cholinesterase combines in its active surface an anionic and an esteratic site, similar to true cholinesterase. It has been demonstrated that butyrylcholinesterase (BCHE) may have a greater role in cholinergic transmission than previously surmised, making BChE inhibition an important therapeutic goal in Alzheimer's disease.

    BCHE/Butyrylcholinesterase Alternative Name

    acylcholine acylhydrolase,butyrylcholine esterase,BCHE,Butyrylcholinesterase,CHE1,choline esterase II,cholinesterase,cholinesterase 1,E1,pseudocholinesterase, [human]
    C730038G20Rik,choline esterase II,acylcholine acylhydrolase,Bche,butyrylcholine esterase,Butyrylcholinesterase,cholinesterase,MGC107651,pseudocholinesterase, [mouse]

    BCHE/Butyrylcholinesterase Related Studies

  • Lockridge O. (1988) Structure of human serum cholinesterase. Bio Essays. 9(4):125-8.
  • Mesulam M, et al. (2002) Widely Spread Butyrylcholinesterase Can Hydrolyze Acetylcholine in the Normal and Alzheimer Brain. Neurobiology of Disease. 9(1): 88-93.
  • Nicolet Y, et al. (2003) Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products. The Journal of Biological Chemistry. 278: 41141-7.
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