Butyrylcholinesterase: Difference between revisions

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Butyrylcholinesterase (HGNC symbol BCHE), also known as BChE, BuChE, pseudocholinesterase, or plasma (cholin)esterase,^[1] is a nonspecific cholinesterase enzyme that hydrolyses many different choline-based esters. In humans, it is made in the liver, found mainly in blood plasma, and encoded by the BCHE gene.^[2]

It is very similar to the neuronal acetylcholinesterase, which is also known as RBC or erythrocyte cholinesterase.^[1] The term "serum cholinesterase" is generally used in reference to a clinical test that reflects levels of both of these enzymes in the blood.^[1] Assay of butyrylcholinesterase activity in plasma can be used as a liver function test as both hypercholinesterasemia and hypocholinesterasemia indicate pathological processes. The half-life of BCHE is approximately 10 to 14 days.^[3]

Butyrylcholine is a synthetic compound that does not occur in the body naturally. It is used as a tool to distinguish between acetylcholinesterase and butyrylcholinesterase.

Clinical significance

Pseudocholinesterase deficiency results in delayed metabolism of only a few compounds of clinical significance, including the following: succinylcholine, mivacurium, procaine, heroin, and cocaine. Of these, its most clinically important substrate is the depolarizing neuromuscular blocking agent, succinylcholine, which the pseudocholinesterase enzyme hydrolyzes to succinylmonocholine and then to succinic acid.

In individuals with normal plasma levels of normally functioning pseudocholinesterase enzyme, hydrolysis and inactivation of approximately 90-95% of an intravenous dose of succinylcholine occurs before it reaches the neuromuscular junction. The remaining 5-10% of the succinylcholine dose acts as an acetylcholine receptor agonist at the neuromuscular junction, causing prolonged depolarization of the postsynaptic junction of the motor-end plate. This depolarization initially triggers fasciculation of skeletal muscle. As a result of prolonged depolarization, endogenous acetylcholine released from the presynaptic membrane of the motor neuron does not produce any additional change in membrane potential after binding to its receptor on the myocyte. Flaccid paralysis of skeletal muscles develops within 1 minute. In normal subjects, skeletal muscle function returns to normal approximately 5 minutes after a single bolus injection of succinylcholine as it passively diffuses away from the neuromuscular junction. Pseudocholinesterase deficiency can result in higher levels of intact succinylcholine molecules reaching receptors in the neuromuscular junction, causing the duration of paralytic effect to continue for as long as 8 hours. This condition is recognized clinically when paralysis of the respiratory and other skeletal muscles fails to spontaneously resolve after succinylcholine is administered as an adjunctive paralytic agent during anesthesia procedures. In such cases respiratory assistance is required.^[4]

In 2008, an experimental new drug was discovered for the potential treatment of cocaine abuse and overdose based on the pseudocholinesterase structure (it was a human BChE mutant with improved catalytic efficiency). It was shown to remove cocaine from the body 2000 times as fast as the natural form of BChE. Studies in rats have shown that the drug prevented convulsions and death when administered cocaine overdoses.^[5] This enzyme also metabolizes succinylcholine which accounts for its rapid degradation in the liver and plasma. There may be genetic variability in the kinetics of this enzyme that can lead to prolonged muscle blockade and potentially dangerous respiratory depression that needs to be treated with assisted ventilation.

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.^[6]

Finally, pseudocholinesterase metabolism of procaine results in formation of paraaminobenzoic acid (PABA). If the patient receiving procaine is on sulfonamide antibiotics such as bactrim the antibiotic effect will be antagonized by providing a new source of PABA to the microbe for subsequent synthesis of folic acid.

Prophylactic countermeasure against nerve gas

Butyrylcholinesterase is a prophylactic countermeasure against organophosphate nerve agents. It binds nerve agent in the bloodstream before it can exert effects in the nervous system. Because it is a biological scavenger (and universal target), it is currently the only therapeutic agent effective in providing complete stoichiometric protection against the entire spectrum of organophosphate nerve agents.^[7]

Physiological role

It was recently indicated that butyrylcholinesterase could be a physiological ghrelin regulator.^[8]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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<imagemap> Image:IrinotecanPathway_WP229.png

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|{{{bSize}}}px|alt=Irinotecan Pathway edit]]

Irinotecan Pathway edit

↑ The interactive pathway map can be edited at WikiPathways: "IrinotecanPathway_WP46359".

Inhibitors

Cymserine and derivatives
Profenamine
Rivastigmine
Tacrine
(+)-ZINC-12613047: IC₅₀ human BChE 13nM, high selectivity over AChE.^[9]

Nomenclature

The nomenclatural variations of BCHE and of cholinesterases generally are discussed at Cholinesterase § Types and nomenclature.

References

↑ ^1.0 ^1.1 ^1.2 Jasmin L (2013-05-28). "Cholinesterase - blood". University of Maryland Medical Center.
↑ Allderdice PW, Gardner HA, Galutira D, Lockridge O, LaDu BN, McAlpine PJ (Oct 1991). "The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26". Genomics. 11 (2): 452–4. doi:10.1016/0888-7543(91)90154-7. PMID 1769657.
↑ Whittaker M (1980). "Plasma cholinesterase variants and the anaesthetist". Anaesthesia. 35 (2): 174–197. doi:10.1111/j.1365-2044.1980.tb03800.x. PMID 6992635.
↑ "Pseudocholinesterase Deficiency". Medscape. WebMD LLC.
↑ Zheng F, Yang W, Ko MC, Liu J, Cho H, Gao D, Tong M, Tai HH, Woods JH, Zhan CG (Sep 2008). "Most efficient cocaine hydrolase designed by virtual screening of transition states". Journal of the American Chemical Society. 130 (36): 12148–55. doi:10.1021/ja803646t. PMC 2646118. PMID 18710224. Lay summary – ScienceDaily.
↑ "Entrez Gene: BCHE butyrylcholinesterase".
↑ "Medical Identification and Treatment Systems(MITS)". Joint Program Executive Office for Chemical and Biological Defense. United States Army.
↑ Chen VP, Gao Y, Geng L, Parks RJ, Pang YP, Brimijoin S (Feb 2015). "Plasma butyrylcholinesterase regulates ghrelin to control aggression". Proceedings of the National Academy of Sciences of the United States of America. 112 (7): 2251–6. doi:10.1073/pnas.1421536112. PMC 4343161. PMID 25646463.
↑ Brus B, Košak U, Turk S, Pišlar A, Coquelle N, Kos J, Stojan J, Colletier JP, Gobec S (Oct 2014). "Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor". Journal of Medicinal Chemistry. 57 (19): 8167–79. doi:10.1021/jm501195e. PMID 25226236.

External links

Butyrylcholinesterase at the US National Library of Medicine Medical Subject Headings (MeSH)
Human BCHE genome location and BCHE gene details page in the UCSC Genome Browser.

[WikiPathways-9] The interactive pathway map can be edited at WikiPathways: "IrinotecanPathway_WP46359".

[umm_serum-1] 1.0 ^1.1 ^1.2 Jasmin L (2013-05-28). "Cholinesterase - blood". University of Maryland Medical Center.

[pmid1769657-2] Allderdice PW, Gardner HA, Galutira D, Lockridge O, LaDu BN, McAlpine PJ (Oct 1991). "The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26". Genomics. 11 (2): 452–4. doi:10.1016/0888-7543(91)90154-7. PMID 1769657.

[pmid6992635-3] Whittaker M (1980). "Plasma cholinesterase variants and the anaesthetist". Anaesthesia. 35 (2): 174–197. doi:10.1111/j.1365-2044.1980.tb03800.x. PMID 6992635.

[urlPseudocholinesterase_Deficiency-4] "Pseudocholinesterase Deficiency". Medscape. WebMD LLC.

[pmid18710224-5] Zheng F, Yang W, Ko MC, Liu J, Cho H, Gao D, Tong M, Tai HH, Woods JH, Zhan CG (Sep 2008). "Most efficient cocaine hydrolase designed by virtual screening of transition states". Journal of the American Chemical Society. 130 (36): 12148–55. doi:10.1021/ja803646t. PMC 2646118. PMID 18710224. Lay summary – ScienceDaily.

[6] "Entrez Gene: BCHE butyrylcholinesterase".

[urlMedical_Identification_and_Treatment_Systems(MITS)-7] "Medical Identification and Treatment Systems(MITS)". Joint Program Executive Office for Chemical and Biological Defense. United States Army.

[8] Chen VP, Gao Y, Geng L, Parks RJ, Pang YP, Brimijoin S (Feb 2015). "Plasma butyrylcholinesterase regulates ghrelin to control aggression". Proceedings of the National Academy of Sciences of the United States of America. 112 (7): 2251–6. doi:10.1073/pnas.1421536112. PMC 4343161. PMID 25646463.

[pmid25226236-10] Brus B, Košak U, Turk S, Pišlar A, Coquelle N, Kos J, Stojan J, Colletier JP, Gobec S (Oct 2014). "Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor". Journal of Medicinal Chemistry. 57 (19): 8167–79. doi:10.1021/jm501195e. PMID 25226236.

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[§ 1]

[9]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+'''Butyrylcholinesterase''' ([[HUGO Gene Nomenclature Committee|HGNC]] symbol '''BCHE'''), [[#Nomenclature|also known as]] '''BChE''', '''BuChE''', '''pseudocholinesterase''', or '''plasma (cholin)esterase''',<ref name=umm_serum>{{cite web | url = http://www.umm.edu/ency/article/003358.htm | title = Cholinesterase - blood | author = Jasmin L | publisher = University of Maryland Medical Center | date = 2013-05-28 }}</ref> is a nonspecific [[cholinesterase]] enzyme that hydrolyses many different [[choline]]-based [[ester]]s. In humans, it is made in the liver, found mainly in [[blood plasma]], and encoded by the ''BCHE'' [[gene]].<ref name="pmid1769657">{{cite journal | vauthors = Allderdice PW, Gardner HA, Galutira D, Lockridge O, LaDu BN, McAlpine PJ | title = The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26 | journal = Genomics | volume = 11 | issue = 2 | pages = 452–4 | date = Oct 1991 | pmid = 1769657 | doi = 10.1016/0888-7543(91)90154-7 }}</ref>
-{{GNF_Protein_box
- | image = PBB_Protein_BCHE_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p0i.
- | PDB = {{PDB2|1p0i}}, {{PDB2|1p0m}}, {{PDB2|1p0p}}, {{PDB2|1p0q}}, {{PDB2|1xlu}}, {{PDB2|1xlv}}, {{PDB2|1xlw}}, {{PDB2|2j4c}}
- | Name = Butyrylcholinesterase
- | HGNCid = 983
- | Symbol = BCHE
- | AltSymbols =; CHE1; E1
- | OMIM = 177400
- | ECnumber = 3.1.1.8
- | Homologene = 20065
- | MGIid = 894278
- | GeneAtlas_image1 = PBB_GE_BCHE_205433_at_tn.png
- | Function = {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0004104 |text = cholinesterase activity}} {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}}
- | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005641 |text = nuclear envelope lumen}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
- | Process = {{GNF_GO|id=GO:0050783 |text = cocaine metabolic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 590
-    | Hs_Ensembl = ENSG00000114200
-    | Hs_RefseqProtein = NP_000046
-    | Hs_RefseqmRNA = NM_000055
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 3
-    | Hs_GenLoc_start = 166973387
-    | Hs_GenLoc_end = 167037944
-    | Hs_Uniprot = P06276
-    | Mm_EntrezGene = 12038
-    | Mm_Ensembl = ENSMUSG00000027792
-    | Mm_RefseqmRNA = NM_009738
-    | Mm_RefseqProtein = NP_033868
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 3
-    | Mm_GenLoc_start = 73721734
-    | Mm_GenLoc_end = 73794168
-    | Mm_Uniprot = Q499C7
-  }}
-}}
-'''Butyrylcholinesterase''', also known as '''BCHE''', is a human [[gene]]. Butyrylcholinesterase is also called serum cholinesterase. It is very similar to the neuronal acetylcholinesterase. Butyrylcholine is a synthetic compound and does not occur in the body naturally. It is used as a tool to distinguish between acetyl- and butyrylcholinesterase.
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+It is very similar to the neuronal [[acetylcholinesterase]], which is also known as RBC or erythrocyte cholinesterase.<ref name=umm_serum /> The term "serum cholinesterase" is generally used in reference to a clinical test that reflects levels of both of these enzymes in the blood.<ref name=umm_serum /> Assay of butyrylcholinesterase activity in plasma can be used as a [[liver function test]] as both hypercholinesterasemia and hypocholinesterasemia indicate pathological processes. The half-life of BCHE is approximately 10 to 14 days.<ref name="pmid6992635">{{cite journal | vauthors = Whittaker M | title = Plasma cholinesterase variants and the anaesthetist | journal = Anaesthesia | volume = 35 | issue = 2 | pages = 174–197 | year = 1980 | pmid = 6992635 | doi = 10.1111/j.1365-2044.1980.tb03800.x }}</ref>
-{{PBB_Summary
-| section_title =
-| summary_text = 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.<ref>{{cite web | title = Entrez Gene: BCHE butyrylcholinesterase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=590| accessdate = }}</ref>
-}}
-==See also==
+[[Butyrylcholine]] is a synthetic compound that does not occur in the body naturally. It is used as a tool to distinguish between acetylcholinesterase and butyrylcholinesterase.
-[[Cholinesterase enzyme]]
-==References==
+==Clinical significance==
-{{reflist|2}}
+[[Pseudocholinesterase deficiency]] results in delayed metabolism of only a few compounds of clinical significance, including the following: [[succinylcholine]], [[mivacurium]], [[procaine]], [[heroin]], and [[cocaine]]. Of these, its most clinically important substrate is the depolarizing neuromuscular blocking agent, [[succinylcholine]], which the pseudocholinesterase enzyme hydrolyzes to succinylmonocholine and then to succinic acid.
+In individuals with normal plasma levels of normally functioning pseudocholinesterase enzyme, hydrolysis and inactivation of approximately 90-95% of an intravenous dose of succinylcholine occurs before it reaches the neuromuscular junction. The remaining 5-10% of the succinylcholine dose acts as an acetylcholine receptor agonist at the neuromuscular junction, causing prolonged depolarization of the postsynaptic junction of the motor-end plate. This depolarization initially triggers [[fasciculation]] of skeletal muscle. As a result of prolonged depolarization, endogenous acetylcholine released from the presynaptic membrane of the motor neuron does not produce any additional change in membrane potential after binding to its receptor on the myocyte. Flaccid paralysis of skeletal muscles develops within 1 minute. In normal subjects, skeletal muscle function returns to normal approximately 5 minutes after a single bolus injection of succinylcholine as it passively diffuses away from the neuromuscular junction. Pseudocholinesterase deficiency can result in higher levels of intact succinylcholine molecules reaching receptors in the neuromuscular junction, causing the duration of paralytic effect to continue for as long as 8 hours. This condition is recognized clinically when paralysis of the respiratory and other skeletal muscles fails to spontaneously resolve after succinylcholine is administered as an adjunctive paralytic agent during anesthesia procedures. In such cases respiratory assistance is required.<ref name="urlPseudocholinesterase Deficiency">{{cite web | url = http://emedicine.medscape.com/article/247019-overview+emedicine.medscape.com | title = Pseudocholinesterase Deficiency | publisher = WebMD LLC | work = Medscape | accessdate = }}</ref>
-==Further reading==
+In 2008, an experimental new drug was discovered for the potential treatment of [[cocaine]] abuse and overdose based on the pseudocholinesterase structure (it was a human BChE mutant with improved catalytic efficiency). It was shown to remove cocaine from the body 2000 times as fast as the natural form of BChE. Studies in rats have shown that the drug prevented [[convulsions]] and death when administered cocaine overdoses.<ref name="pmid18710224">{{cite journal | vauthors = Zheng F, Yang W, Ko MC, Liu J, Cho H, Gao D, Tong M, Tai HH, Woods JH, Zhan CG | title = Most efficient cocaine hydrolase designed by virtual screening of transition states | journal = Journal of the American Chemical Society | volume = 130 | issue = 36 | pages = 12148–55 | date = Sep 2008 | pmid = 18710224 | pmc = 2646118 | doi = 10.1021/ja803646t | laysummary = http://www.sciencedaily.com/releases/2008/09/080915164427.htm | laysource = ScienceDaily }}</ref> This enzyme also metabolizes [[succinylcholine]] which accounts for its rapid degradation in the liver and plasma. There may be genetic variability in the kinetics of this enzyme that can lead to prolonged muscle blockade and potentially dangerous respiratory depression that needs to be treated with assisted ventilation.
-{{refbegin | 2}}
-{{PBB_Further_reading
+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.<ref>{{cite web |title = Entrez Gene: BCHE butyrylcholinesterase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=590| accessdate = }}</ref>
-| citations =
-*{{cite journal  | author=Lockridge O |title=Structure of human serum cholinesterase. |journal=Bioessays |volume=9 |issue= 4 |pages= 125-8 |year= 1989 |pmid= 3067729 |doi= 10.1002/bies.950090406 }}
+Finally, pseudocholinesterase metabolism of [[procaine]] results in formation of [[paraaminobenzoic acid]] (PABA). If the patient receiving procaine is on [[sulfonamide (medicine)|sulfonamide]] antibiotics such as [[bactrim]] the antibiotic effect will be antagonized by providing a new source of PABA to the microbe for subsequent synthesis of [[folic acid]].
-*{{cite journal  | author=Allderdice PW, Gardner HA, Galutira D, ''et al.'' |title=The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26. |journal=Genomics |volume=11 |issue= 2 |pages= 452-4 |year= 1992 |pmid= 1769657 |doi=  }}
-*{{cite journal  | author=Gaughan G, Park H, Priddle J, ''et al.'' |title=Refinement of the localization of human butyrylcholinesterase to chromosome 3q26.1-q26.2 using a PCR-derived probe. |journal=Genomics |volume=11 |issue= 2 |pages= 455-8 |year= 1992 |pmid= 1769658 |doi=  }}
+===Prophylactic countermeasure against nerve gas===
-*{{cite journal  | author=Arpagaus M, Kott M, Vatsis KP, ''et al.'' |title=Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. |journal=Biochemistry |volume=29 |issue= 1 |pages= 124-31 |year= 1990 |pmid= 2322535 |doi=  }}
+Butyrylcholinesterase is a [[prophylactic]] [[countermeasure]] against [[organophosphate]] [[nerve agent]]s. It binds nerve agent in the bloodstream before it can exert effects in the nervous system. Because it is a biological scavenger (and universal target), it is currently the only therapeutic agent effective in providing complete [[stoichiometry|stoichiometric]] protection against the entire spectrum of organophosphate nerve agents.<ref name="urlMedical Identification and Treatment Systems(MITS)">{{cite web | url = http://www.jpeocbd.osd.mil/packs/Default.aspx?pg=1207 | title = Medical Identification and Treatment Systems(MITS) | format = | work = Joint Program Executive Office for Chemical and Biological Defense   | publisher = United States Army }}</ref>
-*{{cite journal  | author=Nogueira CP, McGuire MC, Graeser C, ''et al.'' |title=Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117 (GGT----GGAG). |journal=Am. J. Hum. Genet. |volume=46 |issue= 5 |pages= 934-42 |year= 1990 |pmid= 2339692 |doi=  }}
-*{{cite journal  | author=McGuire MC, Nogueira CP, Bartels CF, ''et al.'' |title=Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 953-7 |year= 1989 |pmid= 2915989 |doi=  }}
+=== Physiological role ===
-*{{cite journal  | author=Prody CA, Zevin-Sonkin D, Gnatt A, ''et al.'' |title=Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 11 |pages= 3555-9 |year= 1987 |pmid= 3035536 |doi=  }}
-*{{cite journal  | author=Lockridge O, Adkins S, La Du BN |title=Location of disulfide bonds within the sequence of human serum cholinesterase. |journal=J. Biol. Chem. |volume=262 |issue= 27 |pages= 12945-52 |year= 1987 |pmid= 3115973 |doi=  }}
+It was recently indicated that butyrylcholinesterase could be a physiological ghrelin regulator.<ref>{{cite journal | vauthors = Chen VP, Gao Y, Geng L, Parks RJ, Pang YP, Brimijoin S | title = Plasma butyrylcholinesterase regulates ghrelin to control aggression | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 112 | issue = 7 | pages = 2251–6 | date = Feb 2015 | pmid = 25646463 | doi = 10.1073/pnas.1421536112 | pmc=4343161}}</ref>
-*{{cite journal  | author=McTiernan C, Adkins S, Chatonnet A, ''et al.'' |title=Brain cDNA clone for human cholinesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 19 |pages= 6682-6 |year= 1987 |pmid= 3477799 |doi=  }}
-*{{cite journal  | author=Lockridge O, Bartels CF, Vaughan TA, ''et al.'' |title=Complete amino acid sequence of human serum cholinesterase. |journal=J. Biol. Chem. |volume=262 |issue= 2 |pages= 549-57 |year= 1987 |pmid= 3542989 |doi=  }}
+==Interactive pathway map==
-*{{cite journal  | author=Jbilo O, Toutant JP, Vatsis KP, ''et al.'' |title=Promoter and transcription start site of human and rabbit butyrylcholinesterase genes. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20829-37 |year= 1994 |pmid= 8063698 |doi=  }}
+{{IrinotecanPathway_WP229|highlight=Butyrylcholinesterase}}
-*{{cite journal  | author=Mattes C, Bradley R, Slaughter E, Browne S |title=Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters. |journal=Life Sci. |volume=58 |issue= 13 |pages= PL257-61 |year= 1996 |pmid= 8622553 |doi=  }}
-*{{cite journal  | author=Iida S, Kinoshita M, Fujii H, ''et al.'' |title=Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. |journal=Hum. Mutat. |volume=6 |issue= 4 |pages= 349-51 |year= 1996 |pmid= 8680411 |doi= 10.1002/humu.1380060411 }}
+== Inhibitors ==
-*{{cite journal  | author=Kamendulis LM, Brzezinski MR, Pindel EV, ''et al.'' |title=Metabolism of cocaine and heroin is catalyzed by the same human liver carboxylesterases. |journal=J. Pharmacol. Exp. Ther. |volume=279 |issue= 2 |pages= 713-7 |year= 1996 |pmid= 8930175 |doi=  }}
+* [[Cymserine]] and derivatives
-*{{cite journal  | author=Hidaka K, Iuchi I, Tomita M, ''et al.'' |title=Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency. |journal=Ann. Hum. Genet. |volume=61 |issue= Pt 6 |pages= 491-6 |year= 1998 |pmid= 9543549 |doi= 10.1046/j.1469-1809.1997.6160491.x }}
+* [[Profenamine]]
-*{{cite journal  | author=Browne SP, Slaughter EA, Couch RA, ''et al.'' |title=The influence of plasma butyrylcholinesterase concentration on the in vitro hydrolysis of cocaine in human plasma. |journal=Biopharmaceutics & drug disposition |volume=19 |issue= 5 |pages= 309-14 |year= 1998 |pmid= 9673783 |doi=  }}
+* [[Rivastigmine]]
-*{{cite journal  | author=Altamirano CV, Lockridge O |title=Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers. |journal=Biochemistry |volume=38 |issue= 40 |pages= 13414-22 |year= 1999 |pmid= 10529218 |doi=  }}
+* [[Tacrine]]
-*{{cite journal  | author=Darvesh S, Kumar R, Roberts S, ''et al.'' |title=Butyrylcholinesterase-Mediated enhancement of the enzymatic activity of trypsin. |journal=Cell. Mol. Neurobiol. |volume=21 |issue= 3 |pages= 285-96 |year= 2002 |pmid= 11569538 |doi=  }}
+* (+)-ZINC-12613047: IC<sub>50</sub> human BChE 13nM, high selectivity over [[AChE]].<ref name="pmid25226236">{{cite journal | vauthors = Brus B, Košak U, Turk S, Pišlar A, Coquelle N, Kos J, Stojan J, Colletier JP, Gobec S | title = Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor | journal = Journal of Medicinal Chemistry | volume = 57 | issue = 19 | pages = 8167–79 | date = Oct 2014 | pmid = 25226236 | doi = 10.1021/jm501195e }}</ref>
-*{{cite journal  | author=Barta C, Sasvari-Szekely M, Devai A, ''et al.'' |title=Analysis of mutations in the plasma cholinesterase gene of patients with a history of prolonged neuromuscular block during anesthesia. |journal=Mol. Genet. Metab. |volume=74 |issue= 4 |pages= 484-8 |year= 2002 |pmid= 11749053 |doi= 10.1006/mgme.2001.3251 }}
-}}
+==Nomenclature==
+The nomenclatural variations of BCHE and of cholinesterases generally are discussed at ''[[Cholinesterase#Types and nomenclature|Cholinesterase § Types and nomenclature]]''.
+== See also ==
+*[[Cholinesterase]]s
+* [[Dibucaine number]]
+== References ==
+{{reflist|35em}}
+== Further reading ==
+{{refbegin|35em}}
+* {{cite journal | vauthors = Bodur E, Cokugras AN | title = The effects of indole-3-acetic acid on human and horse serum butyrylcholinesterase | journal = Chemico-Biological Interactions | volume = 157–158 | issue = 16 | pages = 375–378 | date = Dec 2005 | pmid = 16429500 | doi = 10.1016/j.cbi.2005.10.061 }}
+* {{cite journal | vauthors = Lockridge O | title = Structure of human serum cholinesterase | journal = BioEssays | volume = 9 | issue = 4 | pages = 125–8 | date = Oct 1988 | pmid = 3067729 | doi = 10.1002/bies.950090406 }}
+* {{cite journal | vauthors = Allderdice PW, Gardner HA, Galutira D, Lockridge O, LaDu BN, McAlpine PJ | title = The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26 | journal = Genomics | volume = 11 | issue = 2 | pages = 452–4 | date = Oct 1991 | pmid = 1769657 | doi = 10.1016/0888-7543(91)90154-7 }}
+* {{cite journal | vauthors = Gaughan G, Park H, Priddle J, Craig I, Craig S | title = Refinement of the localization of human butyrylcholinesterase to chromosome 3q26.1-q26.2 using a PCR-derived probe | journal = Genomics | volume = 11 | issue = 2 | pages = 455–8 | date = Oct 1991 | pmid = 1769658 | doi = 10.1016/0888-7543(91)90155-8 }}
+* {{cite journal | vauthors = Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O | title = Structure of the gene for human butyrylcholinesterase. Evidence for a single copy | journal = Biochemistry | volume = 29 | issue = 1 | pages = 124–31 | date = Jan 1990 | pmid = 2322535 | doi = 10.1021/bi00453a015 }}
+* {{cite journal | vauthors = Nogueira CP, McGuire MC, Graeser C, Bartels CF, Arpagaus M, Van der Spek AF, Lightstone H, Lockridge O, La Du BN | title = Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117 (GGT----GGAG) | journal = American Journal of Human Genetics | volume = 46 | issue = 5 | pages = 934–42 | date = May 1990 | pmid = 2339692 | pmc = 1683584 | doi =  }}
+* {{cite journal | vauthors = McGuire MC, Nogueira CP, Bartels CF, Lightstone H, Hajra A, Van der Spek AF, Lockridge O, La Du BN | title = Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 3 | pages = 953–7 | date = Feb 1989 | pmid = 2915989 | pmc = 286597 | doi = 10.1073/pnas.86.3.953 }}
+* {{cite journal | vauthors = Prody CA, Zevin-Sonkin D, Gnatt A, Goldberg O, Soreq H | title = Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 11 | pages = 3555–9 | date = Jun 1987 | pmid = 3035536 | pmc = 304913 | doi = 10.1073/pnas.84.11.3555 }}
+* {{cite journal | vauthors = Lockridge O, Adkins S, La Du BN | title = Location of disulfide bonds within the sequence of human serum cholinesterase | journal = The Journal of Biological Chemistry | volume = 262 | issue = 27 | pages = 12945–52 | date = Sep 1987 | pmid = 3115973 | doi =  }}
+* {{cite journal | vauthors = McTiernan C, Adkins S, Chatonnet A, Vaughan TA, Bartels CF, Kott M, Rosenberry TL, La Du BN, Lockridge O | title = Brain cDNA clone for human cholinesterase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 19 | pages = 6682–6 | date = Oct 1987 | pmid = 3477799 | pmc = 299147 | doi = 10.1073/pnas.84.19.6682 }}
+* {{cite journal | vauthors = Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL | title = Complete amino acid sequence of human serum cholinesterase | journal = The Journal of Biological Chemistry | volume = 262 | issue = 2 | pages = 549–57 | date = Jan 1987 | pmid = 3542989 | doi =  }}
+* {{cite journal | vauthors = Jbilo O, Toutant JP, Vatsis KP, Chatonnet A, Lockridge O | title = Promoter and transcription start site of human and rabbit butyrylcholinesterase genes | journal = The Journal of Biological Chemistry | volume = 269 | issue = 33 | pages = 20829–37 | date = Aug 1994 | pmid = 8063698 | doi =  }}
+* {{cite journal | vauthors = Mattes C, Bradley R, Slaughter E, Browne S | title = Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters | journal = Life Sciences | volume = 58 | issue = 13 | pages = PL257–61 | year = 1996 | pmid = 8622553 | doi = 10.1016/0024-3205(96)00065-3 }}
+* {{cite journal | vauthors = Iida S, Kinoshita M, Fujii H, Moriyama Y, Nakamura Y, Yura N, Moriwaki K | title = Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia | journal = Human Mutation | volume = 6 | issue = 4 | pages = 349–51 | year = 1996 | pmid = 8680411 | doi = 10.1002/humu.1380060411 }}
+* {{cite journal | vauthors = Kamendulis LM, Brzezinski MR, Pindel EV, Bosron WF, Dean RA | title = Metabolism of cocaine and heroin is catalyzed by the same human liver carboxylesterases | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 279 | issue = 2 | pages = 713–7 | date = Nov 1996 | pmid = 8930175 | doi =  }}
+* {{cite journal | vauthors = Hidaka K, Iuchi I, Tomita M, Watanabe Y, Minatogawa Y, Iwasaki K, Gotoh K, Shimizu C | title = Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency | journal = Annals of Human Genetics | volume = 61 | issue = Pt 6 | pages = 491–6 | date = Nov 1997 | pmid = 9543549 | doi = 10.1046/j.1469-1809.1997.6160491.x }}
+* {{cite journal | vauthors = Browne SP, Slaughter EA, Couch RA, Rudnic EM, McLean AM | title = The influence of plasma butyrylcholinesterase concentration on the in vitro hydrolysis of cocaine in human plasma | journal = Biopharmaceutics & Drug Disposition | volume = 19 | issue = 5 | pages = 309–14 | date = Jul 1998 | pmid = 9673783 | doi = 10.1002/(SICI)1099-081X(199807)19:5<309::AID-BDD108>3.0.CO;2-9 }}
+* {{cite journal | vauthors = Altamirano CV, Lockridge O | title = Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers | journal = Biochemistry | volume = 38 | issue = 40 | pages = 13414–22 | date = Oct 1999 | pmid = 10529218 | doi = 10.1021/bi991475 }}
+* {{cite journal | vauthors = Darvesh S, Kumar R, Roberts S, Walsh R, Martin E | title = Butyrylcholinesterase-Mediated enhancement of the enzymatic activity of trypsin | journal = Cellular and Molecular Neurobiology | volume = 21 | issue = 3 | pages = 285–96 | date = Jun 2001 | pmid = 11569538 | doi = 10.1023/A:1010947205224 }}
+* {{cite journal | vauthors = Barta C, Sasvari-Szekely M, Devai A, Kovacs E, Staub M, Enyedi P | title = Analysis of mutations in the plasma cholinesterase gene of patients with a history of prolonged neuromuscular block during anesthesia | journal = Molecular Genetics and Metabolism | volume = 74 | issue = 4 | pages = 484–8 | date = Dec 2001 | pmid = 11749053 | doi = 10.1006/mgme.2001.3251 }}
 {{refend}}
-{{protein-stub}}
+== External links ==
+*{{MeshName|Butyrylcholinesterase}}
+* {{UCSC gene info|BCHE}}
+{{PDB Gallery|geneid=590}}
+{{Esterases}}
+{{Neurotransmitter metabolism enzymes}}
+{{Acetylcholine metabolism and transport modulators}}
+[[Category:Enzymes]]