View source for CYP2E1

{{Infobox_gene}}
'''Cytochrome P450 2E1''' (abbreviated '''CYP2E1''', {{EC number|1.14.13.n7}}) is a member of the [[cytochrome P450]] mixed-function oxidase system, which is involved in the metabolism of [[xenobiotic]]s in the body. This class of enzymes is divided up into a number of subcategories, including CYP1, CYP2, and CYP3, which as a group are largely responsible for the breakdown of foreign compounds in mammals.<ref name="Lewis_2003">{{cite journal | vauthors = Lewis DF, Lake BG, Bird MG, Loizou GD, Dickins M, Goldfarb PS | title = Homology modelling of human CYP2E1 based on the CYP2C5 crystal structure: investigation of enzyme-substrate and enzyme-inhibitor interactions | journal = Toxicology in Vitro | volume = 17 | issue = 1 | pages = 93–105 | date = Feb 2003 | pmid = 12537967 | doi=10.1016/s0887-2333(02)00098-x}}</ref>

The CYP2 subfamily is responsible for the majority of P450-mediated drug metabolism in humans.<ref name="Lewis_2003"/> While CYP2E1 itself carries out a relatively low number of these reactions (~4% of known P450-mediated drug oxidations), it and related enzymes [[CYP1A2]] and [[CYP3A4]] are responsible for the breakdown of a large number of toxic environmental chemicals and carcinogens that enter the body, in addition to basic metabolic reactions such as fatty acid oxidations.<ref name="Rendic_1997">{{cite journal | vauthors = Rendic S, Di Carlo FJ | title = Human cytochrome P450 enzymes: a status report summarizing their reactions, substrates, inducers, and inhibitors | journal = Drug Metabolism Reviews | volume = 29 | issue = 1–2 | pages = 413–580 | pmid = 9187528 | year = 1997 | doi=10.3109/03602539709037591}}</ref>

== Function ==

CYP2E1 is a [[membrane protein]] expressed in high levels in the liver, where it composes nearly 50% of the total hepatic cytochrome P450 mRNA<ref name="Bièche_2007">{{cite journal | vauthors = Bièche I, Narjoz C, Asselah T, Vacher S, Marcellin P, Lidereau R, Beaune P, de Waziers I | title = Reverse transcriptase-PCR quantification of mRNA levels from cytochrome (CYP)1, CYP2 and CYP3 families in 22 different human tissues | journal = Pharmacogenetics and Genomics | volume = 17 | issue = 9 | pages = 731–42 | date = Sep 2007 | pmid = 17700362 | doi = 10.1097/FPC.0b013e32810f2e58 }}</ref> and 7% of the hepatic cytochrome P450 protein.<ref name="Shimada_1994">{{cite journal | vauthors = Shimada T, Yamazaki H, Mimura M, Inui Y, Guengerich FP | title = Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 270 | issue = 1 | pages = 414–23 | date = Jul 1994 | pmid = 8035341 }}</ref> The liver is therefore where most drugs undergo deactivation by CYP2E1, either directly or by facilitated [[excretion]] from the body.

CYP2E1 metabolizes mostly small, polar molecules, including toxic laboratory chemicals such as [[dimethylformamide]], [[aniline]], and [[Haloalkane|halogenated hydrocarbons]] ''(see table below)''. While these oxidations are often of benefit to the body, certain [[carcinogen]]s and [[toxin]]s a<nowiki/>re [[bioactivated]] by CYP2E1, implicating the enzyme in the onset of [[hepatotoxicity]] caused by certain classes of drugs ''(see disease relevance section below).''

CYP2E1 also plays a role in several important metabolic reactions, including the conversion of ethanol to [[acetaldehyde]] and to [[acetate]] in humans,<ref name="pmid1778977">{{cite journal | vauthors = Hayashi S, Watanabe J, Kawajiri K | title = Genetic polymorphisms in the 5'-flanking region change transcriptional regulation of the human cytochrome P450IIE1 gene | journal = Journal of Biochemistry | volume = 110 | issue = 4 | pages = 559–65 | date = Oct 1991 | pmid = 1778977 | doi =  }}</ref> where it works alongside [[alcohol dehydrogenase]] and [[aldehyde dehydrogenase]]. In the conversion sequence of [[acetyl-CoA]] to glucose, CYP2E1 transforms [[acetone]] via [[hydroxyacetone]] (acetol) into [[propylene glycol]] and [[methylglyoxal]], the precursors of [[pyruvate]], [[acetate]] and [[lactic acid|lactate]].<ref name="Glew2010">{{cite web|url=http://www.bioline.org.br/request?np10002|author=Glew, Robert H|title=You Can Get There From Here: Acetone, Anionic Ketones and Even-Carbon Fatty Acids can Provide Substrates for Gluconeogenesis|accessdate=March 8, 2014}}</ref><ref>{{cite journal | vauthors = Miller ON, Bazzano G | title = Propanediol metabolism and its relation to lactic acid metabolism | journal = Annals of the New York Academy of Sciences | volume = 119 | issue = 3 | pages = 957–73 | date = Jul 1965 | pmid = 4285478 | doi = 10.1111/j.1749-6632.1965.tb47455.x | bibcode = 1965NYASA.119..957M }}</ref><ref>{{cite journal | vauthors = Ruddick JA | year = 1972 | title = Toxicology, metabolism, and biochemistry of 1,2-propanediol | journal = Toxicol Appl Pharmacol | volume = 21 | pages = 102–111 | doi = 10.1016/0041-008X(72)90032-4}}</ref>

CYP2E1 also carries out the metabolism of endogenous fatty acids such as the ω-1 hydroxylation of fatty acids such as [[arachidonic acid]], involving it in important signaling pathways that may link it to diabetes and obesity.<ref name="Porubsky_2008">{{cite journal | vauthors = Porubsky PR, Meneely KM, Scott EE | title = Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates | journal = The Journal of Biological Chemistry | volume = 283 | issue = 48 | pages = 33698–707 | date = Nov 2008 | pmid = 18818195 | pmc = 2586265 | doi = 10.1074/jbc.M805999200 }}</ref> Thus, it acts as a monooxygenase to metabolize [[arachidonic acid]] to 19-hydroxyeicosatetraenoic acid (19-HETE) (see [[20-Hydroxyeicosatetraenoic acid]]). However, it also acts as an [[epoxygenase]] activity to metabolize [[docosahexaenoic acid]] to [[epoxide]]s, primarily 19''R'',20''S''-epoxyeicosapentaenoic acid and 19''S'',20''R''-epoxyeicosapentaenoic acid isomers (termed 19,20-EDP) and [[eicosapentaenoic acid]] to epoxides, primarily 17''R'',18''S''-eicosatetraenic acid and 17''S'',18''R''-eicosatetraenic acid isomers (termed 17,18-EEQ).<ref>{{cite journal | vauthors = Westphal C, Konkel A, Schunck WH | title = CYP-eicosanoids--a new link between omega-3 fatty acids and cardiac disease? | journal = Prostaglandins & Other Lipid Mediators | volume = 96 | issue = 1–4 | pages = 99–108 | date = Nov 2011 | pmid = 21945326 | doi = 10.1016/j.prostaglandins.2011.09.001 }}</ref> 19-HETE is an inhibitor of 20-HETE, a broadly active signaling molecule, e.g. it constricts [[arteriole]]s, elevates blood pressure, promotes [[inflammation]] responses, and stimulates the growth of various types of tumor cells; however the in vivo ability and significance of 19-HETE in inhibiting 20-HETE has not been demonstrated (see [[20-Hydroxyeicosatetraenoic acid]]). The EDP (see [[Epoxydocosapentaenoic acid]]) and EEQ (see [[epoxyeicosatetraenoic acid]]) metabolites have a broad range of activities. In various animal models and in vitro studies on animal and human tissues, they decrease hypertension and pain perception; suppress inflammation; inhibit [[angiogenesis]], endothelial cell migration and endothelial cell proliferation; and inhibit the growth and metastasis of human breast and prostate cancer cell lines.<ref name="ReferenceA">{{cite journal | vauthors = Fleming I | title = The pharmacology of the cytochrome P450 epoxygenase/soluble epoxide hydrolase axis in the vasculature and cardiovascular disease | journal = Pharmacological Reviews | volume = 66 | issue = 4 | pages = 1106–40 | date = Oct 2014 | pmid = 25244930 | doi = 10.1124/pr.113.007781 }}</ref><ref>{{cite journal | vauthors = Zhang G, Kodani S, Hammock BD | title = Stabilized epoxygenated fatty acids regulate inflammation, pain, angiogenesis and cancer | journal = Progress in Lipid Research | volume = 53 | pages = 108–23 | date = Jan 2014 | pmid = 24345640 | pmc = 3914417 | doi = 10.1016/j.plipres.2013.11.003 }}</ref><ref>{{cite journal | vauthors = He J, Wang C, Zhu Y, Ai D | title = Soluble epoxide hydrolase: A potential target for metabolic diseases | journal = Journal of Diabetes | volume = 8 | issue = 3 | pages = 305–13 | date = Dec 2015 | pmid = 26621325 | doi = 10.1111/1753-0407.12358 }}</ref><ref name="pmid25240260">{{cite journal | vauthors = Wagner K, Vito S, Inceoglu B, Hammock BD | title = The role of long chain fatty acids and their epoxide metabolites in nociceptive signaling | journal = Prostaglandins & Other Lipid Mediators | volume = 113–115 | pages = 2–12 | date = Oct 2014 | pmid = 25240260 | pmc = 4254344 | doi = 10.1016/j.prostaglandins.2014.09.001 }}</ref> It is suggested that the EDP and EEQ metabolites function in humans as they do in animal models and that, as products of the [[omega-3 fatty acid]]s, docosahexaenoic acid and eicosapentaenoic acid, the EDP and EEQ metabolites contribute to many of the beneficial effects attributed to dietary omega-3 fatty acids.<ref name="ReferenceA"/><ref name="pmid25240260"/><ref>{{cite journal | vauthors = Fischer R, Konkel A, Mehling H, Blossey K, Gapelyuk A, Wessel N, von Schacky C, Dechend R, Muller DN, Rothe M, Luft FC, Weylandt K, Schunck WH | title = Dietary omega-3 fatty acids modulate the eicosanoid profile in man primarily via the CYP-epoxygenase pathway | journal = Journal of Lipid Research | volume = 55 | issue = 6 | pages = 1150–1164 | date = Mar 2014 | pmid = 24634501 | pmc = 4031946 | doi = 10.1194/jlr.M047357 }}</ref>  EDP and EEQ metabolites are short-lived, being inactivated within seconds or minutes of formation by [[epoxide hydrolase]]s, particularly [[soluble epoxide hydrolase]], and therefore act locally. CYP2E1 is not regarded as being a major contributor to forming the cited epoxides<ref name="pmid25240260"/> but could act locally in certain tissues to do so.

=== Substrates ===
Following is a table of selected [[enzyme substrate|substrates]] of CYP2E1. Where classes of agents are listed, there may be exceptions within the class.
{| class="wikitable sortable"
|+'''Selected substrates of CYP2E1'''
|-
! Substrates 
|- style="vertical-align: top;"
| 
* [[anaesthetics]]:
** [[halothane]]<ref name="FASS">[http://www.fass.se/LIF/produktfakta/fakta_lakare_artikel.jsp?articleID=18352 Swedish environmental classification of pharmaceuticals] Facts for prescribers (Fakta för förskrivare)</ref><ref name="Flockhart" />
** [[enflurane]]<ref name="FASS" /><ref name="Flockhart" />
**[[isoflurane]]<ref name="Flockhart">{{cite web |author=Flockhart DA |title=Drug Interactions: Cytochrome P<sub>450</sub> Drug Interaction Table |publisher=[[Indiana University School of Medicine]] |year=2007 |url=http://medicine.iupui.edu/flockhart/table.htm}} Retrieved on July 2011</ref>
**[[methoxyflurane]]<ref name="Flockhart" />
**[[sevoflurane]]<ref name="Flockhart" />
* [[paracetamol]]<ref name="FASS" /> ([[acetaminophen]]) - used as [[analgesic]], [[antipyretic]] - [[toxication]] by CYP2E1<ref name="Flockhart" />
* [[ethanol]]<ref name="FASS" /><ref name="Flockhart" />  ([[psychoactive]])
*Industrial potentially toxic substances
**[[aniline]]<ref name="Flockhart" />
**[[benzene]]<ref name="Flockhart" /> 
**[[dimethylformamide]]<ref name="Flockhart" />
* [[theophylline]]<ref name="Flockhart" /> ([[stimulant]], active [[metabolite]] of [[caffeine]])
* [[chlorzoxazone]]<ref name="Flockhart" /> ([[muscle relaxant]])
* [[Zopiclone]] and [[Eszopiclone]] ([[sedative]]/[[hypnotics]])
|-
|}

== Structure ==
CYP2E1 exhibits structural motifs common to other human membrane-bound [[cytochrome P450]] enzymes, and is composed of 12 major α-helices and 4 β-sheets with short intervening helices interspersed between the two.<ref name="Porubsky_2008"/> Like other [[enzyme]]s of this class, the [[active site]] of CYP2E1 contains an [[iron]] atom bound by a [[heme]] center which mediates the [[electron transfer]] steps necessary to carry out [[Redox|oxidation]] of its substrates. The active site of CYP2E1 is the smallest observed in human P450 enzymes, with its small capacity attributed in part to the introduction of an isoleucine at position 115. The side-chain of this residue protrudes out above the heme center, restricting active site volume compared to related enzymes that have less bulky [[Amino acid|residues]] at this position.<ref name="Porubsky_2008"/> T<sup>303</sup>, which also protrudes into the active site, is particularly important for substrate positioning above the reactive iron center and is hence highly conserved by many cytochrome P450 enzymes.<ref name="Porubsky_2008"/> Its hydroxyl group is well-positioned to donate a [[hydrogen bond]] to potential acceptors on the substrate, and its methyl group has also been implicated in the positioning of fatty acids within the active site.<ref>{{cite journal | vauthors = Fukuda T, Imai Y, Komori M, Nakamura M, Kusunose E, Satouchi K, Kusunose M | title = Replacement of Thr-303 of P450 2E1 with serine modifies the regioselectivity of its fatty acid hydroxylase activity | journal = Journal of Biochemistry | volume = 113 | issue = 1 | pages = 7–12 | date = Jan 1993 | pmid = 8454577 }}</ref><sup>,</sup><ref>{{cite journal | vauthors = Fukuda T, Imai Y, Komori M, Nakamura M, Kusunose E, Satouchi K, Kusunose M | title = Different mechanisms of regioselection of fatty acid hydroxylation by laurate (omega-1)-hydroxylating P450s, P450 2C2 and P450 2E1 | journal = Journal of Biochemistry | volume = 115 | issue = 2 | pages = 338–44 | date = Feb 1994 | pmid = 8206883 }}</ref> A number of residues proximal to the active site including L<sup>368</sup> help make up a constricted, hydrophobic access channel which may also be important for determining the enzyme's specificity towards small molecules and ω-1 hydroxylation of fatty acids.<ref name="Porubsky_2008"/>  [[File:CYP2E1 Active site.png|centre|thumb|302x302px|Selected residues in the active site of CYP2E1. Created using 3E4E (bound to inhibitor 4-methyl pyrazole)]].

==Regulation==

=== Genetic regulation ===
In humans, the CYP2E1 enzyme is encoded by the ''CYP2E1'' [[gene]].<ref name="pmid8307581">{{cite journal | vauthors = Kölble K | title = Regional mapping of short tandem repeats on human chromosome 10: cytochrome P450 gene CYP2E, D10S196, D10S220, and D10S225 | journal = Genomics | volume = 18 | issue = 3 | pages = 702–4 | date = Dec 1993 | pmid = 8307581 | doi = 10.1016/S0888-7543(05)80378-7 }}</ref> The enzyme has been identified in fetal liver, where it is posited to be the predominant ethanol-metabolizing enzyme, and may be connected to ethanol-mediated [[teratogenesis]].<ref>{{cite journal | vauthors = Raucy JL, Schultz ED, Wester MR, Arora S, Johnston DE, Omdahl JL, Carpenter SP | title = Human lymphocyte cytochrome P450 2E1, a putative marker for alcohol-mediated changes in hepatic chlorzoxazone activity | journal = Drug Metabolism and Disposition | volume = 25 | issue = 12 | pages = 1429–35 | date = Dec 1997 | pmid = 9394034 }}</ref> In rats, within one day of birth the hepatic CYP2E1 gene is activated transcriptionally.

CYP2E1 expression is easily inducible, and can occur in the presence of a number of its substrates, including [[ethanol]],<ref name="Flockhart" /> [[isoniazid]],<ref name="Flockhart" /> [[tobacco]],<ref>{{cite journal | vauthors = Desai HD, Seabolt J, Jann MW | title = Smoking in patients receiving psychotropic medications: a pharmacokinetic perspective | journal = CNS Drugs | volume = 15 | issue = 6 | pages = 469–94 | year = 2001 | pmid = 11524025 | doi = 10.2165/00023210-200115060-00005 }}</ref> [[isopropanol]],<ref name="Rendic_1997"/> [[benzene]],<ref name="Rendic_1997"/> [[toluene]],<ref name="Rendic_1997"/> and [[acetone]].<ref name="Rendic_1997"/> For ethanol specifically, it seems that there exist two stages of induction, a post-translational mechanism for increased protein stability at low levels of ethanol and an additional transcriptional induction at high levels of ethanol.<ref name="pmid10397283">{{cite journal | vauthors = Lieber CS | title = Microsomal ethanol-oxidizing system (MEOS): the first 30 years (1968-1998)--a review | journal = Alcoholism, Clinical and Experimental Research | volume = 23 | issue = 6 | pages = 991–1007 | date = Jun 1999 | pmid = 10397283 | doi = 10.1111/j.1530-0277.1999.tb04217.x }}</ref>

=== Chemical regulation ===
CYP2E1 is inhibited by a variety of small molecules, many of which act [[Competitive inhibition|competitively]]. Two such inhibitors, indazole and 4-methylpyrazole, coordinate with the active site's iron atom and were crystallized with recombinant human CYP2E1 in 2008 to give the first true crystal structures of the enzyme.<ref name="Porubsky_2008"/> Other inhibitors include [[diethyldithiocarbamate]]<ref name="FASS" /> (in [[cancer]]), and [[disulfiram]]<ref name="Flockhart" /> (in [[alcoholism]]).

== Disease relevance ==
CYP2E1 is expressed in high levels in the liver, where it works to clear toxins from the body.<ref name="Bièche_2007"/><ref name="Shimada_1994"/> In doing so, CYP2E1 [[Activation|bioactivates]] a variety of common anesthetics, including [[Paracetamol|acetaminophen]], [[halothane]], [[enflurane]], and isoflurane.<ref name="Rendic_1997" /> The oxidation of these molecules by CYP2E1 can produce harmful substances such as [[Trifluoroacetic acid|trifluoroacetic acid chloride]],<ref>{{cite journal | vauthors = Ray DC, Drummond GB | title = Halothane hepatitis | journal = British Journal of Anaesthesia | volume = 67 | issue = 1 | pages = 84–99 | date = Jul 1991 | pmid = 1859766 | doi=10.1093/bja/67.1.84}}</ref> and is a major reason for their observed hepatotoxicity in patients.

CYP2E1 and other cytochrome P450 enzymes can inadvertently produce reactive oxygen species (ROS) in their active site when catalysis is not coordinated correctly, resulting in potential [[lipid peroxidation]] as well as protein and DNA oxidation.<ref name="Porubsky_2008"/> CYP2E1 is particularly susceptible to this phenomenon compared to other P450 enzymes, suggesting that its expression levels may be important for negative physiological effects observed in a number of disease states.<ref name="Porubsky_2008"/>

CYP2E1 expression levels have been correlated with a variety of dietary and physiological factors, such as ethanol consumption,<ref>{{cite journal | vauthors = Nanji AA, Zhao S, Sadrzadeh SM, Dannenberg AJ, Tahan SR, Waxman DJ | title = Markedly enhanced cytochrome P450 2E1 induction and lipid peroxidation is associated with severe liver injury in fish oil-ethanol-fed rats | journal = Alcoholism, Clinical and Experimental Research | volume = 18 | issue = 5 | pages = 1280–5 | date = Oct 1994 | pmid = 7847620 | doi=10.1111/j.1530-0277.1994.tb00119.x}}</ref> diabetes,<ref>{{cite journal | vauthors = Koide CL, Collier AC, Berry MJ, Panee J | title = The effect of bamboo extract on hepatic biotransforming enzymes--findings from an obese-diabetic mouse model | journal = Journal of Ethnopharmacology | volume = 133 | issue = 1 | pages = 37–45 | date = Jan 2011 | pmid = 20832461 | pmc = 3471658 | doi = 10.1016/j.jep.2010.08.062 }}</ref> fasting,<ref>{{cite journal | vauthors = Johansson I, Ekström G, Scholte B, Puzycki D, Jörnvall H, Ingelman-Sundberg M | title = Ethanol-, fasting-, and acetone-inducible cytochromes P-450 in rat liver: regulation and characteristics of enzymes belonging to the IIB and IIE gene subfamilies | journal = Biochemistry | volume = 27 | issue = 6 | pages = 1925–34 | date = Mar 1988 | pmid = 3378038 | doi=10.1021/bi00406a019}}</ref> and obesity.<ref>{{cite journal | vauthors = Raucy JL, Lasker JM, Kraner JC, Salazar DE, Lieber CS, Corcoran GB | title = Induction of cytochrome P450IIE1 in the obese overfed rat | journal = Molecular Pharmacology | volume = 39 | issue = 3 | pages = 275–80 | date = Mar 1991 | pmid = 2005876 }}</ref> It appears that cellular levels of the enzyme may be controlled by the molecular chaperone [[Hsp90|HSP90]], which upon association with CYP2E1 allows for transport to the [[proteasome]] and subsequent degradation. Ethanol and other substrates may disrupt this association, leading to the higher expression levels observed in their presence.<ref>{{cite journal | vauthors = Kitam VO, Maksymchuk OV, Chashchyn MO | title = The possible mechanisms of CYP2E1 interactions with HSP90 and the influence of ethanol on them | language = en | journal = BMC Structural Biology | volume = 12 | issue = 1 | pages = 33 | date = 2012-12-17 | pmid = 23241420 | pmc = 3544703 | doi = 10.1186/1472-6807-12-33 }}</ref> The increased expression of CYP2E1 accompanying these health conditions may therefore contribute to their [[pathogenesis]] by increasing the rate of production of ROS in the body.<ref name="Porubsky_2008"/>

==Applications==
Trees have been genetically engineered to overexpress the CYP2E1 enzyme.  These [[transgenic]] trees have been used to remove pollutants from groundwater, a process known as [[phytoremediation]].<ref name="pmid17940038">{{cite journal | vauthors = Doty SL, James CA, Moore AL, Vajzovic A, Singleton GL, Ma C, Khan Z, Xin G, Kang JW, Park JY, Meilan R, Strauss SH, Wilkerson J, Farin F, Strand SE | title = Enhanced phytoremediation of volatile environmental pollutants with transgenic trees | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 43 | pages = 16816–21 | date = Oct 2007 | pmid = 17940038 | pmc = 2040402 | doi = 10.1073/pnas.0703276104 | bibcode = 2007PNAS..10416816D }}</ref>

== See also ==
*[[Cytochrome]]
*[[Metabolism]]
*[[List of cytochrome P450 modulators]]

== References ==
{{reflist|33em}}

== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Smith G, Stubbins MJ, Harries LW, Wolf CR | title = Molecular genetics of the human cytochrome P450 monooxygenase superfamily | journal = Xenobiotica | volume = 28 | issue = 12 | pages = 1129–65 | date = Dec 1998 | pmid = 9890157 | doi = 10.1080/004982598238868 }}
* {{cite journal | vauthors = Kessova I, Cederbaum AI | title = CYP2E1: biochemistry, toxicology, regulation and function in ethanol-induced liver injury | journal = Current Molecular Medicine | volume = 3 | issue = 6 | pages = 509–18 | date = Sep 2003 | pmid = 14527082 | doi = 10.2174/1566524033479609 }}
* {{cite journal | vauthors = Webb A, Lind PA, Kalmijn J, Feiler HS, Smith TL, Schuckit MA, Wilhelmsen K | title = The investigation into CYP2E1 in relation to the level of response to alcohol through a combination of linkage and association analysis | journal = Alcoholism, Clinical and Experimental Research | volume = 35 | issue = 1 | pages = 10–8 | date = Jan 2011 | pmid = 20958328 | doi = 10.1111/j.1530-0277.2010.01317.x | pmc=3005010}}
{{refend}}

==External links==
* {{UCSC gene info|CYP2E1}}

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{{Dioxygenases}}
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[[Category:Cytochrome P450]]
[[Category:EC 1.14.13]]