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<title>Biochemistry, Pseudocholinesterase - StatPearls - NCBI Bookshelf</title>
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<meta name="robots" content="INDEX,FOLLOW,NOARCHIVE" /><meta name="citation_inbook_title" content="StatPearls [Internet]" /><meta name="citation_title" content="Biochemistry, Pseudocholinesterase" /><meta name="citation_publisher" content="StatPearls Publishing" /><meta name="citation_date" content="2022/09/24" /><meta name="citation_author" content="Andrew Benner" /><meta name="citation_author" content="Noble F. Lewallen" /><meta name="citation_author" content="Nazia M. Sadiq" /><meta name="citation_pmid" content="31424868" /><meta name="citation_fulltext_html_url" content="https://www.ncbi.nlm.nih.gov/books/NBK545284/" /><link rel="schema.DC" href="http://purl.org/DC/elements/1.0/" /><meta name="DC.Title" content="Biochemistry, Pseudocholinesterase" /><meta name="DC.Type" content="Text" /><meta name="DC.Publisher" content="StatPearls Publishing" /><meta name="DC.Contributor" content="Andrew Benner" /><meta name="DC.Contributor" content="Noble F. Lewallen" /><meta name="DC.Contributor" content="Nazia M. Sadiq" /><meta name="DC.Date" content="2022/09/24" /><meta name="DC.Identifier" content="https://www.ncbi.nlm.nih.gov/books/NBK545284/" /><meta name="description" content="Pseudocholinesterase is a serine hydrolase enzyme primarily produced in the liver that catalyzes the hydrolysis of choline esters, most prominently succinylcholine and mivacurium.[1] It is crucial to differentiate this enzyme from "true" cholinesterase, also known as acetylcholinesterase. It occurs in higher concentrations within conducting tissues such as the central or peripheral nervous systems and neuromuscular junctions.[2] Due to diverse functions and tissue distribution within the human body, pseudocholinesterase often gets referred to through various enzymatic names, including plasma cholinesterase, serum cholinesterase, acetylcholine acetylhydrolase, and butyrylcholinesterase (BuChE).[3]" /><meta name="og:title" content="Biochemistry, Pseudocholinesterase" /><meta name="og:type" content="book" /><meta name="og:description" content="Pseudocholinesterase is a serine hydrolase enzyme primarily produced in the liver that catalyzes the hydrolysis of choline esters, most prominently succinylcholine and mivacurium.[1] It is crucial to differentiate this enzyme from "true" cholinesterase, also known as acetylcholinesterase. It occurs in higher concentrations within conducting tissues such as the central or peripheral nervous systems and neuromuscular junctions.[2] Due to diverse functions and tissue distribution within the human body, pseudocholinesterase often gets referred to through various enzymatic names, including plasma cholinesterase, serum cholinesterase, acetylcholine acetylhydrolase, and butyrylcholinesterase (BuChE).[3]" /><meta name="og:url" content="https://www.ncbi.nlm.nih.gov/books/NBK545284/" /><meta name="og:site_name" content="NCBI Bookshelf" /><meta name="og:image" content="https://www.ncbi.nlm.nih.gov/corehtml/pmc/pmcgifs/bookshelf/thumbs/th-statpearls-lrg.png" /><meta name="twitter:card" content="summary" /><meta name="twitter:site" content="@ncbibooks" /><meta name="bk-non-canon-loc" content="/books/n/statpearls/article-27927/" /><link rel="canonical" href="https://www.ncbi.nlm.nih.gov/books/NBK545284/" /><link rel="stylesheet" href="/corehtml/pmc/css/figpopup.css" type="text/css" media="screen" /><link rel="stylesheet" href="/corehtml/pmc/css/bookshelf/2.26/css/books.min.css" type="text/css" /><link rel="stylesheet" href="/corehtml/pmc/css/bookshelf/2.26/css/books_print.min.css" type="text/css" /><style type="text/css">p a.figpopup{display:inline !important} .bk_tt {font-family: monospace} .first-line-outdent .bk_ref {display: inline} </style><script type="text/javascript" src="/corehtml/pmc/js/jquery.hoverIntent.min.js"> </script><script type="text/javascript" src="/corehtml/pmc/js/common.min.js?_=3.18"> </script><script type="text/javascript">window.name="mainwindow";</script><script type="text/javascript" src="/corehtml/pmc/js/bookshelf/2.26/book-toc.min.js"> </script><script type="text/javascript" src="/corehtml/pmc/js/bookshelf/2.26/books.min.js"> </script>
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<div class="pre-content"><div><div class="bk_prnt"><p class="small">NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.</p><p>StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2025 Jan-. </p></div></div></div>
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<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK545284_"><span class="title" itemprop="name">Biochemistry, Pseudocholinesterase</span></h1><p class="contrib-group"><h4>Authors</h4><span itemprop="author">Andrew Benner</span><sup>1</sup>; <span itemprop="author">Noble F. Lewallen</span><sup>2</sup>; <span itemprop="author">Nazia M. Sadiq</span>.</p><h4>Affiliations</h4><div class="affiliation"><sup>1</sup> Michigan State University - College of Osteopathic Medicine</div><div class="affiliation"><sup>2</sup> Michigan State University College of Osteopathic Medicine</div><p class="small">Last Update: <span itemprop="dateModified">September 24, 2022</span>.</p></div><div class="body-content whole_rhythm" itemprop="text"><div id="article-27927.s1"><h2 id="_article-27927_s1_">Introduction</h2><p>Pseudocholinesterase is a serine hydrolase enzyme primarily produced in the liver that catalyzes the hydrolysis of choline esters, most prominently succinylcholine and mivacurium.<a class="bk_pop" href="#article-27927.r1">[1]</a> It is crucial to differentiate this enzyme from "true" cholinesterase, also known as acetylcholinesterase. It occurs in higher concentrations within conducting tissues such as the central or peripheral nervous systems and neuromuscular junctions.<a class="bk_pop" href="#article-27927.r2">[2]</a> Due to diverse functions and tissue distribution within the human body, pseudocholinesterase often gets referred to through various enzymatic names, including plasma cholinesterase, serum cholinesterase, acetylcholine acetylhydrolase, and butyrylcholinesterase (BuChE).<a class="bk_pop" href="#article-27927.r3">[3]</a></p><p>In addition to possessing multiple names, the enzyme exists in many pharmacogenetic variations, with BuChE operating as the primary human cholinesterase form. When comparing concentrations within the human plasma, the ratio of pseudocholinesterase (BuChE) to true cholinesterase (AChE) overwhelmingly favors BuChE by a ratio of 1000 to 1.<a class="bk_pop" href="#article-27927.r3">[3]</a></p></div><div id="article-27927.s2"><h2 id="_article-27927_s2_">Fundamentals</h2><p>BuChE functions primarily as a serine hydrolase that catalyzes the hydrolysis of choline and noncholine esters and maintains active aryl acrylamide, amplifying the action of trypsin and other proteases within the body.<a class="bk_pop" href="#article-27927.r4">[4]</a> BuChE predominately influences the activity of neurons, specifically within the hippocampus, amygdala, thalamus, and different deep layers of the cerebral cortex.<a class="bk_pop" href="#article-27927.r4">[4]</a> BuChE appears to serve a functional role in the maturation of the central and peripheral nervous systems through regulating neuronal growth and cellular proliferation, especially at the onset of differentiation and throughout the early stages of neuronal development.<a class="bk_pop" href="#article-27927.r5">[5]</a></p></div><div id="article-27927.s3"><h2 id="_article-27927_s3_">Issues of Concern</h2><p>Pseudocholinesterase (butyrylcholine esterase) deficiency causes increased sensitivity to choline ester muscle relaxant medications: succinylcholine and mivacurium. In correlation to the level/variant of BuChE deficiency, patients exposed to these neuromuscular blockade agents may experience an amplified duration of apnea and paralysis ranging from mild to extreme.<a class="bk_pop" href="#article-27927.r6">[6]</a> In the presence of BuChE deficiency, the usual course of action for succinylcholine-induced paralysis gets prolonged from approximately 4 to 6 minutes to up to 8 hours. These patients may also exhibit significant sensitivity to agricultural pesticides (organophosphates), cocaine, and ester local anesthetics, such as procaine.<a class="bk_pop" href="#article-27927.r6">[6]</a></p><p>Should persistent respiratory depression occur, most commonly due to succinylcholine administration in the presence of BuChE deficiency, the mainstay of therapy focuses on prolonged ventilatory support. Positive pressure ventilation is required until skeletal muscle regains adequate neuromuscular function following passive diffusion of succinylcholine from the neuromuscular junction.<a class="bk_pop" href="#article-27927.r7">[7]</a> Patients with known BuChE deficiency status should disclose this information to all medical personnel through a medical alert band, notifying clinicians of increased sensitivity to mivacurium and succinylcholine in case an emergency arises. </p></div><div id="article-27927.s4"><h2 id="_article-27927_s4_">Molecular Level
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</h2><p>The coding gene for BuChE coincides with multiple polymorphisms, resulting in wide variability in the level of activity of each variant, including silent variants with little to no enzymatic function.<a class="bk_pop" href="#article-27927.r4">[4]</a> Depending on the type and location of the gene mutation, alterations in enzyme structure/function or cessation of enzyme synthesis may occur. Specifically, point mutations alter the enzyme's structure due to changes in the mRNA and amino acids compiled during enzyme production, often resulting in abnormal function. Meanwhile, mutations that result in a stop codon or frameshift often lead to dysfunctional enzyme synthesis. Within each molecular form of pseudocholinesterase, there are several sub-variants, defined by the number and orientation of subunits within the molecule; ranging from single monomers (G1) to 2 symmetric monomers (dimer, G2) to dimers conjoined by disulfide bridges (tetramer, G4).<a class="bk_pop" href="#article-27927.r8">[8]</a></p></div><div id="article-27927.s5"><h2 id="_article-27927_s5_">Testing</h2><p>The diagnosis of pseudocholinesterase deficiency most commonly occurs through family history and clinical context of prolonged apnea and paralysis following depolarizing neuromuscular blockade via succinylcholine. With an autosomal recessive inheritance pattern and a heterozygous gene frequency ranging from 1 in 25 to 1 in 50, family members of known homozygotes must undergo testing for the presence of an altered BCHE gene.<a class="bk_pop" href="#article-27927.r9">[9]</a> Confirmation of BuChE deficiency may occur through gene sequencing of the coding gene, <i>BCHE</i>, located at 3q26.1, via techniques such as deletion or duplication analysis, targeted variant analysis, or sequence analysis of the entire gene coding region.</p></div><div id="article-27927.s6"><h2 id="_article-27927_s6_">Pathophysiology</h2><p>The onset of pseudocholinesterase deficiency may occur through inheritable (genetic) or acquired pathways. Despite its etiology, pseudocholinesterase deficiency usually does not have clinically significant effects until the enzyme activity decreases to less than 75% of normal activity levels.<a class="bk_pop" href="#article-27927.r10">[10]</a></p><p>The genetic inheritance of pseudocholinesterase deficiency occurs through an autosomal recessive pattern, with frequencies of approximately 1 in 50 to 1 in 3000 individuals for heterozygotes and homozygotes, respectively.<a class="bk_pop" href="#article-27927.r9">[9]</a> The prevalence of BuChE deficiency is highest amongst those with European ancestry and lowest within the Asian population.</p><p>Acquired conditions that decrease the activity of the BuChE enzyme include malnutrition, advanced age, malignancy, liver or kidney disease, pregnancy, burns, and organophosphate poisoning. In contrast, obesity and chronic alcoholism are suspected to increase pseudocholinesterase activity levels. Medications such as aspirin, metoclopramide, monoamine oxidase inhibitors, oral contraceptives, and anticholinesterase agents may also influence the enzyme's activity.<a class="bk_pop" href="#article-27927.r9">[9]</a> Through hydrolysis and sequestration of toxic compounds, the broad substrate specificity of BuChE may protect against numerous inhaled and administered substances.<a class="bk_pop" href="#article-27927.r11">[11]</a></p></div><div id="article-27927.s7"><h2 id="_article-27927_s7_">Clinical Significance</h2><p>There is conflicting evidence as to whether pseudocholinesterase deficiency plays a role in the progression of Alzheimer's disease. However, increased levels of BuChE and altered structure or function of the enzyme are observable in patients with Alzheimer disease, specifically within the pathognomonic amyloid plaques and neurofibrillary tangles.<a class="bk_pop" href="#article-27927.r4">[4]</a> Furthermore, BuChE may exhibit a synergistic role with ApoE4 in causing mild cognitive impairment.<a class="bk_pop" href="#article-27927.r12">[12]</a></p><p>Plasma cholinesterase levels were significantly higher in patients with drug addictions (most notably, cocaine) than those without, suggesting it serves a significant role in addiction pathophysiology.<a class="bk_pop" href="#article-27927.r13">[13]</a> BuChE gene amplification and elevated enzyme activities are also prevalent in tumorigenesis and neuronal disorders, potentially allowing researchers to target gene expression as a unique treatment modality.<a class="bk_pop" href="#article-27927.r5">[5]</a></p><p>Hepatocytes function as the primary synthesis pathway for plasma cholinesterase. Serum levels of plasma cholinesterase may serve as a valuable biomarker of liver function with an excellent correlation to the currently accepted standards of serum albumin, prothrombin time/international normalized ratio, and MELD score (Model for End-Stage Liver Disease).<a class="bk_pop" href="#article-27927.r14">[14]</a> Levels of serum cholinesterase may also serve as a prognostic marker for advanced liver disease secondary to distinguishing between decompensated and compensated cirrhosis, reflected by low and high enzyme levels, respectively.<a class="bk_pop" href="#article-27927.r14">[14]</a> In addition to its association with liver function, BuChE may also correlate significantly with the role of red blood cells and kidneys.<a class="bk_pop" href="#article-27927.r3">[3]</a><a class="bk_pop" href="#article-27927.r15">[15]</a></p></div><div id="article-27927.s8"><h2 id="_article-27927_s8_">Review Questions</h2><ul><li class="half_rhythm"><div>
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</div></li></ul></div><div id="article-27927.s9"><h2 id="_article-27927_s9_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="article-27927.r1">Yang HS, Goudsouzian N, Martyn JA. Pseudocholinesterase-mediated hydrolysis is superior to neostigmine for reversal of mivacurium-induced paralysis in vitro. <span><span class="ref-journal">Anesthesiology. </span>1996 Apr;<span class="ref-vol">84</span>(4):936-44.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/8638849" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8638849</span></a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="article-27927.r2">Colović MB, Krstić DZ, Lazarević-Pašti TD, Bondžić AM, Vasić VM. Acetylcholinesterase inhibitors: pharmacology and toxicology. <span><span class="ref-journal">Curr Neuropharmacol. </span>2013 May;<span class="ref-vol">11</span>(3):315-35.</span> [<a href="/pmc/articles/PMC3648782/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3648782</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/24179466" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 24179466</span></a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="article-27927.r3">Tunsaringkarn T, Zapuang K, Rungsiyothin A. The Correlative Study of Serum Pseudo-cholinesterase, Biological Parameters and Symptoms Among Occupational Workers. <span><span class="ref-journal">Indian J Clin Biochem. </span>2013 Oct;<span class="ref-vol">28</span>(4):396-402.</span> [<a href="/pmc/articles/PMC3783904/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3783904</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/24426243" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 24426243</span></a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="article-27927.r4">Darvesh S, Hopkins DA, Geula C. Neurobiology of butyrylcholinesterase. <span><span class="ref-journal">Nat Rev Neurosci. </span>2003 Feb;<span class="ref-vol">4</span>(2):131-8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12563284" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12563284</span></a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="article-27927.r5">Mack A, Robitzki A. The key role of butyrylcholinesterase during neurogenesis and neural disorders: an antisense-5'butyrylcholinesterase-DNA study. <span><span class="ref-journal">Prog Neurobiol. </span>2000 Apr;<span class="ref-vol">60</span>(6):607-28.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/10739090" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 10739090</span></a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="article-27927.r6">Kuhnert BR, Philipson EH, Pimental R, Kuhnert PM. A prolonged chloroprocaine epidural block in a postpartum patient with abnormal pseudocholinesterase. <span><span class="ref-journal">Anesthesiology. </span>1982 Jun;<span class="ref-vol">56</span>(6):477-8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/7081736" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 7081736</span></a>]</div></dd><dt>7.</dt><dd><div class="bk_ref" id="article-27927.r7">Williams J, Rosenquist P, Arias L, McCall WV. Pseudocholinesterase deficiency and electroconvulsive therapy. <span><span class="ref-journal">J ECT. </span>2007 Sep;<span class="ref-vol">23</span>(3):198-200.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17805000" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17805000</span></a>]</div></dd><dt>8.</dt><dd><div class="bk_ref" id="article-27927.r8">Atack JR, Perry EK, Bonham JR, Candy JM, Perry RH. 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Butyrylcholinesterase deficiency identified by preoperative patient interview. <span><span class="ref-journal">Korean J Anesthesiol. </span>2013 Dec;<span class="ref-vol">65</span>(6 Suppl):S1-3.</span> [<a href="/pmc/articles/PMC3903816/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3903816</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/24478828" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 24478828</span></a>]</div></dd><dt>10.</dt><dd><div class="bk_ref" id="article-27927.r10">Soliday FK, Conley YP, Henker R. 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Influence of Butyrylcholinesterase in Progression of Mild Cognitive Impairment to Alzheimer's Disease. <span><span class="ref-journal">J Alzheimers Dis. </span>2018;<span class="ref-vol">61</span>(3):1097-1105.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/29254094" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 29254094</span></a>]</div></dd><dt>13.</dt><dd><div class="bk_ref" id="article-27927.r13">Munir S, Habib R, Awan S, Bibi N, Tanveer A, Batool S, Nurulain SM. Biochemical Analysis and Association of Butyrylcholinesterase SNPs rs3495 and rs1803274 with Substance Abuse Disorder. <span><span class="ref-journal">J Mol Neurosci. </span>2019 Mar;<span class="ref-vol">67</span>(3):445-455.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/30707402" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 30707402</span></a>]</div></dd><dt>14.</dt><dd><div class="bk_ref" id="article-27927.r14">Ramachandran J, Sajith KG, Priya S, Dutta AK, Balasubramanian KA. Serum cholinesterase is an excellent biomarker of liver cirrhosis. <span><span class="ref-journal">Trop Gastroenterol. </span>2014 Jan-Mar;<span class="ref-vol">35</span>(1):15-20.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/25276901" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 25276901</span></a>]</div></dd><dt>15.</dt><dd><div class="bk_ref" id="article-27927.r15">Zarday Z, Deery A, Tellis I, Soberman R, Foldes FF. Plasma and red cell cholinesterase activity in uremic patterns (effects of hemodialysis and renal transplantation). <span><span class="ref-journal">J Med. </span>1975;<span class="ref-vol">6</span>(5-6):337-49.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/768397" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 768397</span></a>]</div></dd></dl></div><div><dl class="temp-labeled-list small"><dt></dt><dd><div><p class="no_top_margin">
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<b>Disclosure: </b>Andrew Benner declares no relevant financial relationships with ineligible companies.</p></div></dd><dt></dt><dd><div><p class="no_top_margin">
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<b>Disclosure: </b>Noble Lewallen declares no relevant financial relationships with ineligible companies.</p></div></dd><dt></dt><dd><div><p class="no_top_margin">
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<b>Disclosure: </b>Nazia Sadiq declares no relevant financial relationships with ineligible companies.</p></div></dd></dl></div></div></div>
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