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Inibitore enzimatico Enzymhemmung Inhibitor enzim Inhibidor enzimático Ингибирование ферментов Enzyme inhibitor Inhibice مثبط إنزيم Inhibiteur enzymatique Inhibidor enzimàtic 酶抑制剂 효소 저해제 Inhibitie van enzymen Entzimen inhibitzaile Inibição enzimática 酵素阻害剤
rdfs:comment
Inhibice je v biochemii proces, kdy vazba určité látky způsobí snížení aktivity enzymu. Tím dochází k zamezení či omezení správného průběhu enzymatické reakce. Látky, které takto účinkují, se označují jako enzymatické inhibitory či negativní efektory (opačně zase působí ). Inhibice může být přirozená, která umožňuje regulaci buněčných procesů, a nepřirozená, kdy se v roli inhibitorů ocitají například různé zplodiny metabolismu, ale i léčiva a jedy. Existuje několik typů inhibice, obvykle se uvádí kompetitivní, nekompetitivní, akompetitivní a smíšená, někdy se zvlášť vyčleňuje i ireverzibilní (nevratná) inhibice. 酶抑制剂(英語:Enzyme inhibitor)是一类可以与酶结合并降低其活性的分子。 由于阻断酶的活性可以杀死病原体或纠正代谢失衡,许多药物都是酶抑制剂。 它们也用于杀虫剂。 并非所有与酶结合的分子都是抑制剂; 酶激活剂与酶结合并增加其酶活性,而酶底物结合并在酶的正常催化循环中转化为产物。 一种抑制剂的结合可以阻止进入酶的活性位点和/或阻止酶催化其反应。 抑制剂结合是可逆的或不可逆的。 不可逆抑制剂通常与酶反应并化学改变(例如通过共价键形成)。 这些抑制剂修饰酶活性所需的关键氨基酸残基。 相反,可逆抑制剂非共价结合,并且取决于这些抑制剂是否与酶,和/或酶-底复合物或两者结合,产生不同类型的抑制。 由于抑制特定酶的活性可以杀死病原体或校正新陈代谢的不平衡,许多药物分子都是酶抑制剂,它们的发现和改进是生物化学和药理学研究的一个活跃领域。评判一个药用酶抑制剂通常以它的特异性(不与其他蛋白质结合)及效价(解离常数,表示抑制酶所需的浓度)为指标。高特异性和高效价使药物具有更小的副作用,因而具有更低的毒性。一些酶抑制剂还被用作除草剂或农药。 Ферментативный ингибитор — вещество, замедляющее протекание ферментативной реакции. Различают обратимые и необратимые ингибиторы (см. ниже). Изучение ингибирования ферментов играет важную роль в создании лекарств, в изучении механизма действия и структуры ферментов. Els inhibidors enzimàtics són molècules que uneixen els enzims i fan disminuir la seva activitat. Per mitjà del bloqueig de l'activitat dels enzims, es pot matar un patogen i corregir el desbalanç metabòlic; tal com fan moltes drogues, les quals són inhibidors enzimàtics. Aquests, també, han estat utilitzats com a herbicides i pesticides. No totes les molècules que uneixen als enzims són inhibidors; sinó que també hi ha activadors enzimàtics, molècules que s'uneixen als enzims i incrementen la seva . La unió d'un inhibidor a un enzim pot fer aturar l'entrada del substrat al centre actiu o pot evitar la catalització de la reacció. La substància inhibidora pot ser reversible o irreversible. Els inhibidors irreversibles són aquells que, normalment, en reaccionar amb l'enzim el modifiquen quím Los inhibidores enzimáticos son moléculas que se unen a enzimas y disminuyen su actividad. Puesto que el bloqueo de una enzima puede matar a un agente patógeno o corregir un desequilibrio metabólico, muchos medicamentos actúan como inhibidores enzimáticos. También son usados como herbicidas y pesticidas. Sin embargo, no todas las moléculas que se unen a las enzimas son inhibidores; los activadores enzimáticos se unen a las enzimas e incrementan su actividad. Enzymhemmung (auch Enzyminhibition) ist die Hemmung einer enzymatischen Reaktion durch einen Hemmstoff, der Inhibitor genannt wird. Dabei wird die Geschwindigkeit der katalysierten Reaktion herabgesetzt. Inhibitoren können an unterschiedliche Reaktanten binden, wie zum Beispiel an das Enzym oder das Substrat. Auch der Bindungsort am Enzym kann vom aktiven Zentrum, an dem das Substrat bindet, bis hin zu anderen Stellen, die für die Aktivität des Enzyms wichtig sind, variieren. Enzymhemmung spielt eine wichtige Rolle bei der Regulation des Stoffwechsels in allen Lebewesen. 酵素阻害剤(こうそそがいざい)とは、酵素分子に結合してその活性を低下または消失させる物質のことである。酵素阻害剤は一般に生理活性物質であり、毒性を示すものもあるが、病原体を殺したり、体内の代謝やシグナル伝達などを正常化したりするために医薬品として利用されるものも多い。また殺虫剤や農薬などに利用される種類もある。 酵素に結合する物質すべてが酵素阻害剤というわけではなく、逆に活性を上昇させるもの(酵素活性化剤)もある。 酵素阻害剤の作用には、酵素の基質が活性中心に入って反応が始まるのを阻止するもの、あるいは酵素による反応の触媒作用を阻害するものがある。また酵素に可逆的に結合するもの(濃度が下がれは解離する)と、酵素分子の特定部分と共有結合を形成して不可逆的に結合するものとに分けられる。さらに阻害剤が酵素分子単独、酵素・基質複合体、またその両方に結合するかなどによっても分類される。 生体内にある物質が酵素阻害物質になることもある。例えば、代謝経路の途中にある酵素では、下流の代謝産物により阻害されるものがあり(フィードバック阻害)、これは代謝を調節する機構として働いている。さらに、生物体内にあって生理的機能を持つ酵素阻害タンパク質もある。これらはプロテアーゼやヌクレアーゼなど、生物自身に害を及ぼしうる酵素を厳密に制御する機能を持つものが多い。 مثبطات الإنزيمات (بالإنجليزية: Enzyme inhibitors)‏ هي جزيئات ترتبط بالإنزيمات وتقلل من نشاطها بشكل مؤقت أو دائم. ربط المثبط يمكن أن يوقف المادة الركيزة من دخول موقع الإنزيم النشط و/أو منع الإنزيم من تحفيز تفاعله. وهناك نوعين للمثبطات، اما انعكاسية أو لا انعكاسية. المثبطات اللا انعكاسية عادة تتفاعل مع الانزيم وتغييره كيميائيا (عن طريق تشكيل الروابط التساهمية). هذه المثبطات توجد لتعديل بقايا الأحماض الأمينية الرئيسية اللازمة للنشاط الأنزيمي. في المقابل، يوجد مثبطات انعكاسية التي ترتبط بروابط غير تساهمية، وأنواع مختلفة من المثبطات تـُنتج اعتمادا عما إذا كانت هذه مثبطات لربط إنزيم ما، أو مجموع الانزيم والمادة الركيزة، أو كليهما. العديد من جزيئات الدواء مثبطة للإنزيمات، لذلك فإن اكتشافها وتحسينها هو مجال نشط جدا في بحوث الكيمياء الحيوية والصيدلة. An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction. Um grande número de substâncias pode inibir a atividade enzimática. Algumas dessas substâncias são constituintes da célula e outras são estranhas, levando com a sua presença a alterações significativas do metabolismo. Quando o inibidor é produzido pela própria célula, a variação na sua concentração vai ser muito empregado pela própria célula como uma forma de controle da velocidade das reações. Esse mecanismo vai possibilitar ao organismo responder a diferentes condições fisiológicas. Een inhibitor of enzymremmer is een molecuul dat kan binden aan enzymen en dat daardoor de enzymactiviteit kan verminderen. Enzymen zijn in staat allerlei biochemische reacties efficiënt uit te voeren; ze spelen een cruciale rol in vrijwel alle biologische processen. Door specifieke enzymen te remmen kan de stofwisseling beïnvloed worden. Inhibitie is een essentieel onderdeel van vrijwel alle biochemische processen; biologische systemen bevatten daarom vele soorten inhibitors. Maar er wordt ook veel onderzoek gedaan om nieuwe inhibitors te ontwerpen, te synthetiseren en toe te passen; bijvoorbeeld als geneesmiddel. Con il termine inibitore enzimatico si indica una molecola in grado di instaurare un legame chimico con un enzima, diminuendone così l'attività. L'inibitore infatti può intralciare l'enzima nella catalisi della sua reazione, per esempio impedendo al substrato di entrare nel sito attivo dell'enzima stesso.Il legame tra enzima ed inibitore può essere reversibile o irreversibile. Gli inibitori irreversibili solitamente reagiscono con l'enzima, modificando chimicamente residui amminoacidici fondamentali per l'attività. Al contrario, gli inibitori reversibili si legano non-covalentemente e producono diversi tipi di inibizione a seconda che si leghino all'enzima, al complesso enzima-substrato, o ad entrambi. 효소 저해제(酵素沮害劑, 영어: enzyme inhibitor) 또는 효소 억제제(酵素抑制劑)는 효소와 결합하여 효소-기질 복합체의 형성을 저해함으로써 효소의 촉매 작용을 방해하는 물질로, 효소에 결합하는 부위에 따라 여러 종류로 구분된다. Inhibitor adalah molekul yang dapat menghambat bahkan menghentikan dengan mengotori permukaan katalis. Entzimen inhibitzaileak entzimen jarduera murrizten duten molekulak dira. Molekula horiek naturalak ala artifizialak izan daitezke. Artifizialen artean, esaterako, botika asko daude: molekula hauek mikrobio patogenoen entzimei lotzen dira eta haien jarduera inhibitzen dute, patogenoaren heriotza dakarrena (entzimek ez badute zuzen funtzionatzen bide metaboliko batzuk ez baitira osatzen). Inhibitzaileek entzimen jarduera aldatzen dute, betiko (inhibizio itzulezinaren kasuan) edo aldi baterako (inhibizio itzulgarriaren kasuan). Beraz, bi inhibizio motaz jardun daiteke: Bi mota daude: Un inhibiteur enzymatique est une substance se liant à une enzyme et qui en diminue l'activité. Un inhibiteur peut empêcher la fixation du substrat sur le site actif en se fixant à sa place, ou provoquer une déformation de l'enzyme qui rend celle-ci inactive (inhibiteur allostérique). L'inhibition des enzymes joue un rôle important dans le contrôle des mécanismes biologiques, et notamment dans la régulation des voies métaboliques. Puisque l'inhibition d'une enzyme peut tuer un pathogène ou corriger un déséquilibre métabolique, des applications existent dans de nombreux autres domaines : beaucoup de médicaments, pesticides ou insecticides sont des inhibiteurs enzymatiques. En enzymologie, les inhibiteurs sont très utilisés pour déterminer le mécanisme d'action d'une enzyme. Toutes les moléc
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TGDDF / GDDF MAIs where blue depicts the tetrahydrofolate cofactor analogue, black GAR or thioGAR and red, the connecting atoms. 2 Schematic diagram of the three types of reversible inhibitors. Ritonavir is similar to the natural substrate. Tipranavir is not similar to the natural substrate. Chemical equilibrium reaction formula for competitive, uncompetitive, non-competitive, and mixed inhibition. . Depiction of the reversible chemical equilibria between enzyme + substrate, enzyme/substrate complex, and enzyme + product, and two competing equilibria. The first is between enzyme + inhibitor, enzyme/inhibitor non-covalent complex, followed by irreversible formation of the covalent complex. The second is between enzyme/substrate complex + inhibitor, noncovalent enzyme/substrate, followed by irreversible formation of the covalent complex
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Irreversible inhibitors bind to the enzyme's binding site then undergo a chemical reaction to form a covalent enzyme-inhibitor complex . Binding site in blue, inhibitor in green. Reaction of the irreversible inhibitor diisopropylfluorophosphate with a serine protease Kinetic mechanisms for reversible inhibition. Substrate binding to enzyme in blue, catalysis releasing product in red, inhibitor binding to enzyme in green. Nonpeptidic HIV-1 protease inhibitor tipranavir Schematics for reversible inhibition. Binding site in blue, substrate in black, inhibitor in green, and allosteric site in light green. Chemical mechanism for irreversible inhibition of ornithine decarboxylase by DFMO. Pyridoxal 5'-phosphate and enzyme are not shown. Adapted from Poulin et al, 1992. 60.0 Kinetic mechanism for irreversible inhibition. Substrate binding in blue, catalysis in red, inhibitor binding in green, inactivation reaction in dark green. The coenzyme folic acid compared to the anti-cancer drug methotrexate TGDDF/GDDF multi-substrate adduct inhibitor. Substrate analogue in black, cofactor analogue in blue, non-cleavable linker in red.
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Competitive inhibitors usually bind to the active site. Non-competitive bind to a remote site. Uncompetitive inhibitors only bind once the substrate is bound, fully disrupting catalysis, and mixed inhibition is similar but with only partial disruption of catalysis. Competitive inhibitor examples
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Irreversible inhibition mechanism DFP reaction Inhibition mechanism schematic Methotrexate versus folate DFMO inhibitor mechanism
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DFMO_inhibitor_mechanism.svg DIF reaction.png Ritonavir Schechter Berger Notation.svg Tipranavir structure 2.svg Methotrexate_vs_folate.svg Inhibition schematic .svg Inhibition mechanism .svg TGDDF-GDDF.svg
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酶抑制剂(英語:Enzyme inhibitor)是一类可以与酶结合并降低其活性的分子。 由于阻断酶的活性可以杀死病原体或纠正代谢失衡,许多药物都是酶抑制剂。 它们也用于杀虫剂。 并非所有与酶结合的分子都是抑制剂; 酶激活剂与酶结合并增加其酶活性,而酶底物结合并在酶的正常催化循环中转化为产物。 一种抑制剂的结合可以阻止进入酶的活性位点和/或阻止酶催化其反应。 抑制剂结合是可逆的或不可逆的。 不可逆抑制剂通常与酶反应并化学改变(例如通过共价键形成)。 这些抑制剂修饰酶活性所需的关键氨基酸残基。 相反,可逆抑制剂非共价结合,并且取决于这些抑制剂是否与酶,和/或酶-底复合物或两者结合,产生不同类型的抑制。 由于抑制特定酶的活性可以杀死病原体或校正新陈代谢的不平衡,许多药物分子都是酶抑制剂,它们的发现和改进是生物化学和药理学研究的一个活跃领域。评判一个药用酶抑制剂通常以它的特异性(不与其他蛋白质结合)及效价(解离常数,表示抑制酶所需的浓度)为指标。高特异性和高效价使药物具有更小的副作用,因而具有更低的毒性。一些酶抑制剂还被用作除草剂或农药。 酶抑制剂天然存在并参与代谢调节。例如,代谢途径中的酶可被下游产物抑制。当产物开始积聚时,这种负反馈会减慢生产的速度,并有助于维持细胞稳态。也有的细胞酶抑制剂是特异性结合并抑制标靶酶的蛋白质。这可以帮助控制可能对细胞有害的酶,如蛋白酶和核酸酶。一个典型例子是核糖核酸酶抑制剂,它可以与核糖核酸酶结合,是已知最紧密的蛋白质-蛋白质相互作用之一。天然酶抑制剂也可以作为毒药,用以防御食肉动物或杀死猎物。 효소 저해제(酵素沮害劑, 영어: enzyme inhibitor) 또는 효소 억제제(酵素抑制劑)는 효소와 결합하여 효소-기질 복합체의 형성을 저해함으로써 효소의 촉매 작용을 방해하는 물질로, 효소에 결합하는 부위에 따라 여러 종류로 구분된다. Een inhibitor of enzymremmer is een molecuul dat kan binden aan enzymen en dat daardoor de enzymactiviteit kan verminderen. Enzymen zijn in staat allerlei biochemische reacties efficiënt uit te voeren; ze spelen een cruciale rol in vrijwel alle biologische processen. Door specifieke enzymen te remmen kan de stofwisseling beïnvloed worden. Inhibitie is een essentieel onderdeel van vrijwel alle biochemische processen; biologische systemen bevatten daarom vele soorten inhibitors. Maar er wordt ook veel onderzoek gedaan om nieuwe inhibitors te ontwerpen, te synthetiseren en toe te passen; bijvoorbeeld als geneesmiddel. De moleculaire structuur van een enzym bevat een actief centrum: een locatie waar een stof zich kan binden, om vervolgens door het enzym omgezet te worden in een andere stof. De stof die zich aan een enzym bindt wordt het substraat genoemd. Een inhibitor werkt vaak door op de plaats van het substraat te gaan zitten, waardoor het substraat niet meer kan binden. Een inhibitor kan er ook voor zorgen dat de structuur van het actieve centrum wijzigt, waardoor binding van het substraat eveneens verhinderd wordt. Tegenover inhibitors staan , dit zijn moleculen die enzymactiviteit kunnen verhogen. Inhibitie kan zowel reversibel (omkeerbaar) als irreversibel (onomkeerbaar) zijn. Irreversibele inhibitors werken doorgaans doordat ze reageren met een enzym; het enzym wordt daardoor chemisch veranderd (door de vorming van een covalente verbinding met de inhibitor). Irreversibele inhibitors kunnen belangrijke aminozuurresiduen veranderen, die nodig zijn voor enzymatische activiteit. Reversible inhibitors daarentegen vormen niet-covalente verbindingen met het enzym; er is dan sprake een evenwichtsreactie die door veranderende omstandigheden omgekeerd kan worden. مثبطات الإنزيمات (بالإنجليزية: Enzyme inhibitors)‏ هي جزيئات ترتبط بالإنزيمات وتقلل من نشاطها بشكل مؤقت أو دائم. ربط المثبط يمكن أن يوقف المادة الركيزة من دخول موقع الإنزيم النشط و/أو منع الإنزيم من تحفيز تفاعله. وهناك نوعين للمثبطات، اما انعكاسية أو لا انعكاسية. المثبطات اللا انعكاسية عادة تتفاعل مع الانزيم وتغييره كيميائيا (عن طريق تشكيل الروابط التساهمية). هذه المثبطات توجد لتعديل بقايا الأحماض الأمينية الرئيسية اللازمة للنشاط الأنزيمي. في المقابل، يوجد مثبطات انعكاسية التي ترتبط بروابط غير تساهمية، وأنواع مختلفة من المثبطات تـُنتج اعتمادا عما إذا كانت هذه مثبطات لربط إنزيم ما، أو مجموع الانزيم والمادة الركيزة، أو كليهما. العديد من جزيئات الدواء مثبطة للإنزيمات، لذلك فإن اكتشافها وتحسينها هو مجال نشط جدا في بحوث الكيمياء الحيوية والصيدلة. وكثيرا ما يحكم على مثبط الإنزيم الطبي حسب تصنيفه (افتقاره لرابطة ببروتينات أخرى) وفاعليته (حسب ثابت التفكك الخاص به، الذي يعطي تركيزه الضروري لتثبيط الانزيم). فإذا كانت تلك الخاصتين عالية له فهذا يعني أن الدواء سيكون له آثارا جانبية قليلة، وبالتالي تكون درجة سميتة منخفضة. مثبطات الانزيم تحدث أيضا بشكل طبيعي وتشارك في تنظيم عملية الأيض. على سبيل المثال، الإنزيمات في المسار الأيضي يمكن تثبيطه بالمنتجات التي تنتج خلال سلسلة التفاعلات وتعمل على تثبيطها. هذا النوع من ردود الفعل السلبية يبطئ خط الإنتاج عندما تبدأ المنتجات في البناء وهو وسيلة هامة للحفاظ على التوازن في الخلية. مثبطات الانزيم الخلوية الأخرى هي البروتينات التي ترتبط بالانزيم وتمنع عمله. هذا يمكن أن يساعد في السيطرة على الانزيمات التي قد تكون ضارة للخلية، مثل البروتياز أو نوكليسيس. يمكن أن تستخدم مثبطات الإنزيم الطبيعية كوسيلة للحماية ضد أي جسم غريب أو مؤذي. Los inhibidores enzimáticos son moléculas que se unen a enzimas y disminuyen su actividad. Puesto que el bloqueo de una enzima puede matar a un agente patógeno o corregir un desequilibrio metabólico, muchos medicamentos actúan como inhibidores enzimáticos. También son usados como herbicidas y pesticidas. Sin embargo, no todas las moléculas que se unen a las enzimas son inhibidores; los activadores enzimáticos se unen a las enzimas e incrementan su actividad. La unión de un inhibidor puede impedir la entrada del sustrato al sitio activo de la enzima y/u obstaculizar que la enzima catalice su reacción correspondiente. La unión del inhibidor puede ser reversible o irreversible. Normalmente, los inhibidores irreversibles reaccionan con la enzima de forma covalente y modifican su estructura química a nivel de residuos esenciales de los aminoácidos necesarios para la actividad enzimática. En cambio, los inhibidores reversibles se unen a la enzima de forma no covalente, dando lugar a diferentes tipos de inhibiciones, dependiendo de si el inhibidor se une a la enzima, al complejo enzima-sustrato o a ambos. Muchos medicamentos son inhibidores enzimáticos, por lo que su descubrimiento y mejora es un campo de investigación activo en la bioquímica y la farmacología. La validez de un inhibidor enzimático medicinal suele venir determinada por su especificidad (su incapacidad de unirse a otras proteínas) y su potencia (su constante de disociación, la cual indica la concentración necesaria para inhibir a una enzima). Una alta especificidad y potencia asegura que el medicamento va a tener pocos efectos secundarios y por tanto una baja toxicidad. Los inhibidores enzimáticos también son usados en la naturaleza y están implicados en la regulación del metabolismo. Por ejemplo, las enzimas en una ruta metabólica pueden ser inhibidas por los productos resultantes de sus respectivas rutas. Este tipo de retroalimentación negativa retarda el flujo a través de la ruta cuando los productos comienzan a acumularse y es una manera importante de mantener la homeostasis en una célula. Otros inhibidores enzimáticos celulares son proteínas que se unen específicamente e inhiben una diana enzimática. Esto puede ayudar a controlar enzimas que pueden ser dañinas para la célula, como las proteasas o nucleasas. Un buen ejemplo es el inhibidor de la ribonucleasa, que se une a esta enzima en una de las interacciones proteína-proteína más fuertes conocidas.​ Como inhibidores enzimáticos naturales también cabe destacar los venenos, que son usados como defensa contra los depredadores o como forma de matar a una presa. Ферментативный ингибитор — вещество, замедляющее протекание ферментативной реакции. Различают обратимые и необратимые ингибиторы (см. ниже). Изучение ингибирования ферментов играет важную роль в создании лекарств, в изучении механизма действия и структуры ферментов. Inhibitor adalah molekul yang dapat menghambat bahkan menghentikan dengan mengotori permukaan katalis. Un inhibiteur enzymatique est une substance se liant à une enzyme et qui en diminue l'activité. Un inhibiteur peut empêcher la fixation du substrat sur le site actif en se fixant à sa place, ou provoquer une déformation de l'enzyme qui rend celle-ci inactive (inhibiteur allostérique). L'inhibition des enzymes joue un rôle important dans le contrôle des mécanismes biologiques, et notamment dans la régulation des voies métaboliques. Puisque l'inhibition d'une enzyme peut tuer un pathogène ou corriger un déséquilibre métabolique, des applications existent dans de nombreux autres domaines : beaucoup de médicaments, pesticides ou insecticides sont des inhibiteurs enzymatiques. En enzymologie, les inhibiteurs sont très utilisés pour déterminer le mécanisme d'action d'une enzyme. Toutes les molécules ou ligands se liant à une enzyme ne sont pas des inhibiteurs, les activateurs enzymatiques existent également et accroissent l'activité de l'enzyme. La liaison d'un inhibiteur peut empêcher un substrat de se fixer au site actif de l'enzyme et/ou l'enzyme de catalyser sa réaction. Cette inhibition peut être réversible ou irréversible. Les inhibiteurs irréversibles réagissent généralement avec l'enzyme et la modifient chimiquement. Il se fixent de manière covalente et modifient des résidus amino-acides clés, nécessaires à l'activité enzymatique. En revanche, les inhibiteurs réversibles se lient de façon non covalente et différents types d'inhibition en résultent selon que ces inhibiteurs lient l'enzyme, le complexe enzyme-substrat (ES) ou les deux. Beaucoup de molécules de médicaments sont des inhibiteurs enzymatiques, de sorte que leur découverte et leur amélioration est un domaine de recherche actif en biochimie et en pharmacologie. Un médicament inhibiteur d'enzyme est souvent évalué par sa spécificité (l'absence de liaison à d'autres protéines) et sa puissance (sa constante de dissociation, ou d'inhibition, Ki, qui indique la concentration nécessaire pour inhiber l'enzyme). Une spécificité et une puissance grandes minimisent les effets secondaires d'un médicament et assurent donc une faible toxicité. Ces inhibiteurs sont également produits naturellement et sont impliqués dans la régulation du métabolisme. Par exemple, les enzymes d'une voie métabolique peuvent être inhibées par des produits synthétisés en aval. Cette rétroinhibition ralentit le cours d'un processus au fur et à mesure que les produits s'accumulent et est un moyen important pour le maintien de l'homéostasie dans une cellule. D'autres inhibiteurs d'enzyme cellulaire sont les protéines qui se lient spécifiquement et inhibent une enzyme précise. Ils peuvent aider à contrôler les enzymes qui peuvent être préjudiciables à une cellule, tels que les protéases ou les nucléases, dont un exemple célèbre est l', qui se lie à la ribonucléase dans l'une des plus étroites interactions protéine-protéine connues. Les inhibiteurs enzymatiques naturels peuvent aussi être des poisons et utilisés comme moyens de défense contre les prédateurs ou pour tuer des proies. Um grande número de substâncias pode inibir a atividade enzimática. Algumas dessas substâncias são constituintes da célula e outras são estranhas, levando com a sua presença a alterações significativas do metabolismo. Quando o inibidor é produzido pela própria célula, a variação na sua concentração vai ser muito empregado pela própria célula como uma forma de controle da velocidade das reações. Esse mecanismo vai possibilitar ao organismo responder a diferentes condições fisiológicas. Muitos medicamentos usados rotineiramente baseiam-se na inibição específica de enzimas. O bloqueio de uma única reação vai afetar toda a sequência de reações, já que a reação bloqueada não vai gerar o produto que vai ser necessário pra reações seguintes. Os inibidores podem ser reversíveis ou irreversíveis, de acordo com a estabilidade gerada pela sua ligação com a enzima: * Os inibidores irreversíveis se ligam as enzimas levando a inativação definitiva desta. Estes inibidores são muito tóxicos para o organismo já que não são específicos, sendo capazes de inativar qualquer enzima. * Já os inibidores reversíveis podem ser divididos em dois grupos: os competitivos e os não-competitivos. Essa divisão é baseada na presença ou não de competição entre o inibidor e o substrato pelo centro ativo da enzima. * Os inibidores competitivos competem com o substrato pelo centro ativo da enzima. Estas moléculas apresentam configuração semelhante ao substrato e por isso são capazes de se ligarem ao centro ativo da enzima. Eles produzem um complexo enzima-inibidor que é semelhante ao complexo enzima-substrato. * Os inibidores não-competitivos não tem semelhança estrutural com o substrato de reação que inibem. A sua inibição se dá pela sua ligação a radicais que não pertencem ao grupo ativo. Esta ligação vai alterar a estrutura da enzima e inviabiliza a sua catálise. Inhibice je v biochemii proces, kdy vazba určité látky způsobí snížení aktivity enzymu. Tím dochází k zamezení či omezení správného průběhu enzymatické reakce. Látky, které takto účinkují, se označují jako enzymatické inhibitory či negativní efektory (opačně zase působí ). Inhibice může být přirozená, která umožňuje regulaci buněčných procesů, a nepřirozená, kdy se v roli inhibitorů ocitají například různé zplodiny metabolismu, ale i léčiva a jedy. Existuje několik typů inhibice, obvykle se uvádí kompetitivní, nekompetitivní, akompetitivní a smíšená, někdy se zvlášť vyčleňuje i ireverzibilní (nevratná) inhibice. Mechanismus inhibice je velice rozmanitý. Někdy se inhibitor váže na enzym a zamezuje mu navázat substrát, jindy sice umožní navázání substrátu, ale nemůže dojít k enzymatické reakci. V dalších případech se váže inhibitor až na komplex enzym-substrát (ES) a zamezuje přeměně substrátu. Entzimen inhibitzaileak entzimen jarduera murrizten duten molekulak dira. Molekula horiek naturalak ala artifizialak izan daitezke. Artifizialen artean, esaterako, botika asko daude: molekula hauek mikrobio patogenoen entzimei lotzen dira eta haien jarduera inhibitzen dute, patogenoaren heriotza dakarrena (entzimek ez badute zuzen funtzionatzen bide metaboliko batzuk ez baitira osatzen). Inhibitzaileek entzimen jarduera aldatzen dute, betiko (inhibizio itzulezinaren kasuan) edo aldi baterako (inhibizio itzulgarriaren kasuan). Beraz, bi inhibizio motaz jardun daiteke: 1.- inhibizio itzulgarria: inhibitzaile eta entzimaren arteko lotura ahula denean, erraz banatzen direnean; banatu ostean, entzima guztiz funtzionala da berriz Bi mota daude: * inhibizio lehiakorra: inhibitzaileak itxuraz substratuaren antzeko molekulak dira (gune aktiboari lotzen zaion zatia, behintzat). Inhibitzailea entzimaren gune aktiboan finkatzen da eta substratuak ezin du toki horri atxiki. Lehiakorrak esan nahi du inhibitzailea eta substratua lehian daudela, entzimaren gune aktiboari atxikitzeko. Inhibizio lehiakorrean inhibitzailearen efektua substratuaren kontzentrazioa handituz neutralizatu daiteke. Izan ere, substratu asko dagoenean inhibitzailea entzimaren gune aktiboan lotzeko probabilitatea asko jaisten da. * inhibizio ez-lehiakorra: kasu honetan inhibitzaileak ez du antzik substratuarekin, eta ez da entzimaren gune aktiboan finkatzen. Entzimaren beste toki batean finkatzen da eta -horren ondorioz- gune aktiboaren konformazioa aldatu egiten du, ezinezkoa eginez substratuaren lotura entzimaren gune aktiboan. Hau gertatzen da batez ere entzima alosteriko izeneko entzimekin. 2.- inhibizio itzulezina: inhibitzailea eta entzimaren arteko lotura sendoa da, eta ez da desegiten. Ondorioz, inhibitzailea entzimaren gune aktiboan betiko elkartzen da, eta ez dio substratuari uzten toki horretan sartzen. Inhibizio itzulezina eragiten duten molekulak artifizialak dira gehienak: pozoiak, botikak, intsektizidak, etab. Els inhibidors enzimàtics són molècules que uneixen els enzims i fan disminuir la seva activitat. Per mitjà del bloqueig de l'activitat dels enzims, es pot matar un patogen i corregir el desbalanç metabòlic; tal com fan moltes drogues, les quals són inhibidors enzimàtics. Aquests, també, han estat utilitzats com a herbicides i pesticides. No totes les molècules que uneixen als enzims són inhibidors; sinó que també hi ha activadors enzimàtics, molècules que s'uneixen als enzims i incrementen la seva . La unió d'un inhibidor a un enzim pot fer aturar l'entrada del substrat al centre actiu o pot evitar la catalització de la reacció. La substància inhibidora pot ser reversible o irreversible. Els inhibidors irreversibles són aquells que, normalment, en reaccionar amb l'enzim el modifiquen químicament. Aquests inhibidors, per tant, modifiquen els residus dels aminoàcids que són necessaris per a l'activitat enzimàtica. En canvi, els inhibidors reversibles són aquells que s'uneixen de forma no covalent. No hi ha una sola classe d'inhibidors reversibles; sinó que dins aquest grup hi trobem subgrups segons si la inhibició és produïda per la unió dels inhibidors amb l'enzim, per la seva unió amb el complex substrat-enzim o per unir-se tant a un com a l'altre. Moltes drogues són inhibidors enzimàtics; per tant, el seu descobriment i millorament es troba en l'àrea activa de la recerca de la bioquímica i la farmacologia. Un inhibidor enzimàtic mèdic, és sempre avaluat per la seva especificitat (la seva mancança en la unió a altres proteïnes) i la seva potència (la constant de dissociació que indica la concentració necessària per inhibir l'enzim). Una alta especificitat i potència assegura que la droga tindrà pocs efectes secundaris i una baixa toxicitat. Els inhibidors enzimàtics també són formats a la natura i es troben implicats en el procés de regulació del metabolisme. Per exemple, enzims metabòlics poden ser inhibits per la concentració elevada de substrat. Aquesta classe de feedback negatiu disminueix el flux quan la quantitat de productes és elevada i manté l'homeòstasi a la cèl·lula. Altres inhibidors d'enzims cel·lulars són proteïnes que s'uneixen específicament a la diana de l'enzim. Aquests, poden ajudar en el control d'enzims, com les proteases o nucleases, per tal d'evitar malmetre la cèl·lula. Un bon exemple és l'inhibidor de la ribonucleasa, que uneix a les ribonucleases per mitjà d'interaccions estretes entre proteïnes. Els inhibidors naturals d'enzims, poden ser verinosos i usats com a defensa contra depredadors o com una via per matar presses. Con il termine inibitore enzimatico si indica una molecola in grado di instaurare un legame chimico con un enzima, diminuendone così l'attività. L'inibitore infatti può intralciare l'enzima nella catalisi della sua reazione, per esempio impedendo al substrato di entrare nel sito attivo dell'enzima stesso.Il legame tra enzima ed inibitore può essere reversibile o irreversibile. Gli inibitori irreversibili solitamente reagiscono con l'enzima, modificando chimicamente residui amminoacidici fondamentali per l'attività. Al contrario, gli inibitori reversibili si legano non-covalentemente e producono diversi tipi di inibizione a seconda che si leghino all'enzima, al complesso enzima-substrato, o ad entrambi. Agli enzimi possono legarsi anche molecole in grado di potenziarne l'attività, dette attivatori enzimatici. Alcune di queste molecole non sono indispensabili per la catalisi, ma la loro presenza la facilita. Altri, come i cofattori (es. ioni metallici come calcio, ferro, manganese) e coenzimi (es. prodotti derivanti da vitamine), sono indispensabili e la loro assenza non rende possibile il meccanismo enzimatico. Quindi alcuni inibitori enzimatici possono anche competere per cofattori e coenzimi e ridurre l'attività catalitica in questo modo. Enzymhemmung (auch Enzyminhibition) ist die Hemmung einer enzymatischen Reaktion durch einen Hemmstoff, der Inhibitor genannt wird. Dabei wird die Geschwindigkeit der katalysierten Reaktion herabgesetzt. Inhibitoren können an unterschiedliche Reaktanten binden, wie zum Beispiel an das Enzym oder das Substrat. Auch der Bindungsort am Enzym kann vom aktiven Zentrum, an dem das Substrat bindet, bis hin zu anderen Stellen, die für die Aktivität des Enzyms wichtig sind, variieren. Enzymhemmung spielt eine wichtige Rolle bei der Regulation des Stoffwechsels in allen Lebewesen. An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. Enzyme inhibitors may bind reversibly or irreversibly. Irreversible inhibitors form a chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By contrast, reversible inhibitors bind non-covalently and may spontaneously leave the enzyme, allowing the enzyme to resume its function. Reversible inhibitors produce different types of inhibition depending on whether they bind to the enzyme, the enzyme-substrate complex, or both. Enzyme inhibitors play an important role in all cells, since they are generally specific to one enzyme and serve to control that enzyme's activity. For example, enzymes in a metabolic pathway may be inhibited by molecules produced later in the pathway, thus curtailing the production of molecules that are no longer needed. This type of negative feedback is an important way to maintain balance in a cell. Enzyme inhibitors also control essential enzymes such as proteases or nucleases that, if left unchecked, may damage a cell. Many poisons produced by animals or plants are enzyme inhibitors that block the activity of crucial enzymes in prey or predators. Many drug molecules are enzyme inhibitors that inhibit an aberrant human enzyme or an enzyme critical for the survival of a pathogen such as a virus, bacterium or parasite. Examples include methotrexate (used in chemotherapy and in treating rheumatic arthritis) and the protease inhibitors used to treat HIV/AIDS. Since anti-pathogen inhibitors generally target only one enzyme, such drugs are highly specific and generally produce few side effects in humans, provided that no analogous enzyme is found in humans. (This is often the case, since such pathogens and humans are genetically distant.) Medicinal enzyme inhibitors often have low dissociation constants, meaning that only a minute amount of the inhibitor is required to inhibit the enzyme. A low concentration of the enzyme inhibitor reduces the risk for liver and kidney damage and other adverse drug reactions in humans. Hence the discovery and refinement of enzyme inhibitors is an active area of research in biochemistry and pharmacology. 酵素阻害剤(こうそそがいざい)とは、酵素分子に結合してその活性を低下または消失させる物質のことである。酵素阻害剤は一般に生理活性物質であり、毒性を示すものもあるが、病原体を殺したり、体内の代謝やシグナル伝達などを正常化したりするために医薬品として利用されるものも多い。また殺虫剤や農薬などに利用される種類もある。 酵素に結合する物質すべてが酵素阻害剤というわけではなく、逆に活性を上昇させるもの(酵素活性化剤)もある。 酵素阻害剤の作用には、酵素の基質が活性中心に入って反応が始まるのを阻止するもの、あるいは酵素による反応の触媒作用を阻害するものがある。また酵素に可逆的に結合するもの(濃度が下がれは解離する)と、酵素分子の特定部分と共有結合を形成して不可逆的に結合するものとに分けられる。さらに阻害剤が酵素分子単独、酵素・基質複合体、またその両方に結合するかなどによっても分類される。 生体内にある物質が酵素阻害物質になることもある。例えば、代謝経路の途中にある酵素では、下流の代謝産物により阻害されるものがあり(フィードバック阻害)、これは代謝を調節する機構として働いている。さらに、生物体内にあって生理的機能を持つ酵素阻害タンパク質もある。これらはプロテアーゼやヌクレアーゼなど、生物自身に害を及ぼしうる酵素を厳密に制御する機能を持つものが多い。 酵素阻害剤には、基質と同様に酵素に対する特異性がある場合が多い。一般に医薬品としての阻害剤では、特異性の高い方が毒性・副作用が少ないとされる。また抗菌薬や殺虫剤に求められる選択毒性を出すためにも高い特異性が必要である。
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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dbr:Enzyme_inhibitor
Subject Item
dbr:Drug_metabolism
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dbr:Enzyme_inhibitor
Subject Item
dbr:GABA_analogue
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:GABA_transaminase_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:GMP_synthase
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Gait_(human)
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:HIF_prolyl-hydroxylase_inhibitor
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dbp:mechanismOfAction
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Subject Item
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Subject Item
dbr:Hayflick_limit
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Helicase–primase_complex
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Irosustat
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Irreversible_antagonist
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Lamellar_bodies
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Lanosterol_synthase
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Lipid_signaling
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Liranaftate
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Lone_pair
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:P16
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:PDE1
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Prorenone
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Nitrogen_dioxide_poisoning
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Urokinase_receptor
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dbr:Enzyme_inhibitor
Subject Item
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dbr:Enzyme_inhibitor
Subject Item
dbr:3,4-Dihydroxystyrene
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dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:AEBSF
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Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
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Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Adenosine_monophosphate
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dbr:Enzyme_inhibitor
Subject Item
dbr:Adenosine_triphosphate
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Aiphanes
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Alachlor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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Subject Item
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
n43:sulbactam
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dbr:Enzyme_inhibitor
Subject Item
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Subject Item
dbr:4-hydroxyphenylpyruvate_dioxygenase_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Cyanide
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
dbr:Cycloleucine
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Subject Item
dbr:Cyclophellitol
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Subject Item
dbr:Cyproterone_acetate
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dbr:Enzyme_inhibitor
Subject Item
dbr:Cysteine_protease
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dbr:Enzyme_inhibitor
Subject Item
dbr:DAPT_(chemical)
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dbr:Enzyme_inhibitor
Subject Item
dbr:DHHC_domain
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
dbr:Dacomitinib
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
dbr:EA-4056
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Subject Item
dbr:EC508
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Subject Item
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Subject Item
dbr:Alpha-2-Macroglobulin
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dbr:Enzyme_inhibitor
Subject Item
dbr:Alpha_amylase_inhibitor
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dbr:Enzyme_inhibitor
Subject Item
dbr:Alternative_oxidase
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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dbr:Enzyme_inhibitor
Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
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Subject Item
dbr:Reticulon_4
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:PARP_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:PDE10
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:PDE11
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:PDE9
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Pancreatic_elastase
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:TAX1BP3
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Xanthine_oxidase_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Ribosomally_synthesized_and_post-translationally_modified_peptides
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Monoamine_oxidase_B
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Vitamin-K-epoxide_reductase_(warfarin-sensitive)
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Enzyme_inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:SABIO-Reaction_Kinetics_Database
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Streptomyces_toxytricini
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Targeted_covalent_inhibitors
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Thymidine_phosphorylase
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Steroidogenesis_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Auto_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Feedback_regulation
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Spinocerebellar_ataxia_type_1
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Thermomyces_lanuginosus
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
Subject Item
dbr:Enzyme_Inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Enzyme_inhibitors
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Feedback_inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Gene_expression_regulation,_enzymologic
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Auto-induction
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Auto-inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Auto-inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Reversible_enzyme_inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Reversible_enzyme_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Reversible_inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Reversible_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Inhibition_of_enzymes
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Inhibitory_peptide
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Irreversible_enzyme_inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Irreversible_enzyme_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Irreversible_inhibition
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
dbr:Irreversible_inhibitor
dbo:wikiPageWikiLink
dbr:Enzyme_inhibitor
dbo:wikiPageRedirects
dbr:Enzyme_inhibitor
Subject Item
wikipedia-en:Enzyme_inhibitor
foaf:primaryTopic
dbr:Enzyme_inhibitor