Name: enzyme action and inhibition
Uploaded: 2020-09-24T15:06:50.000Z
Duration: 2 min 34 s
Channel: JoVE

K12 Standards

north-carolina-k-12-science-standard-course-of-study

North Carolina K-12 Science Standard Course of Study

9-12

Chemistry

Matter and its Interactions

PS.Chm.5.1

Enzymes

Enzyme sind biologische Katalysatoren, die die Geschwindigkeit biochemischer Reaktionen beschleunigen. Die meisten Enzyme sind Proteine, die aus Aminosäuren bestehen; während einige RNA-Moleküle sind, die als Ribozyme bekannt sind. 
Enzyme wirken, indem sie die Aktivierungsenergie einer Reaktion senken und dadurch die Reaktionsgeschwindigkeit erhöhen. Sie können sowohl die Synthese als auch den Abbau chemischer Bindungen katalysieren, beeinflussen aber nicht die Richtung oder das Gleichgewicht der Reaktion. 
Jedes Enzym bindet an einen bestimmten Reaktanten, das sogenannte Substrat, und katalysiert eine bestimmte Reaktion. Das Substrat bindet durch Wechselwirkungen wie intermolekulare Kräfte und transiente kovalente Bindungen an eine bestimmte katalytische Region des Enzyms, die als aktives Zentrum bezeichnet wird, was zu einem Enzym-Substrat-Komplex führt.
Diese Bindung ist aufgrund der erforderlichen Konformationskomplementarität zwischen dem Enzym und seinem Substrat hochspezifisch. Daher kann ein bestimmtes Enzym nur auf der Grundlage seiner Konformation spezifische Reaktionen katalysieren. 
Eine einfache Möglichkeit, die Komplexbildung zu verstehen, ist das Schloss-und-Schlüssel-Modell, das davon ausgeht, dass das Substrat in das aktive Zentrum des Enzyms passt, analog zu einem "Schlüssel", der in sein entsprechendes "Schloss" passt. 
Ein anderes Modell, das Induced-Fit-Modell, berücksichtigt jedoch die dynamische Natur des Komplexes. Dieses Modell besagt, dass ein Substrat, wenn es bindet, kleine Konformationsänderungen induziert, was zu einer engeren Passform führt, die die Reaktion begünstigt. 
Die Aktivierungsenergie für eine Reaktion kann durch verschiedene Methoden gesenkt werden. 
Zu den üblichen Mechanismen gehören das Induzieren von Konformationsänderungen im Substrat, die es ermöglichen, eine Bindung leichter aufzubrechen, oder das Zusammenbringen der reaktiven Gruppen zweier Substrate in eine enge Nähe, wodurch die Bindungsbildung gefördert wird. Die Enzymaktivität kann vorübergehend oder dauerhaft durch natürliche oder synthetische Moleküle, sogenannte Inhibitoren, unterdrückt werden.
Zum Beispiel konkurriert ein kompetitiver Inhibitor mit dem Substrat um die Bindung an das aktive Zentrum des Enzyms und verhindert so die Substratbindung.
Auf der anderen Seite bindet ein nicht-kompetitiver Inhibitor an eine andere Stelle des Enzyms, was zu einer Konformationsänderung am aktiven Zentrum führt und die katalytische Aktivität des Enzyms verringert.

enzyme

In lebenden Organismen fungieren Enzyme als Katalysatoren für viele biochemische Reaktionen, die am Zellstoffwechsel beteiligt sind. Die Rolle von Enzymen besteht darin, die Aktivierungsenergien biochemischer Reaktionen zu reduzieren, indem sie mit ihren Substraten Komplexe bilden. Die Senkung der Aktivierungsenergien begünstigt eine Steigerung der Geschwindigkeit biochemischer Reaktionen. Enzymdefizite können oft zu lebensbedrohlichen Krankheiten führen. Beispielsweise beeinträchtigt eine genetische Anomalie, die zu einem Mangel des Enzyms G6PD (Glucose-6-Phosphat-Dehydrogenase) führt, den Stoffwechselweg, der die Zellen mit NADPH versorgt. Eine Störung dieses Stoffwechselwegs kann Glutathion in den roten Blutkörperchen reduzieren und andere Enzyme und Proteine wie Hämoglobin schädigen. Durch die übermäßige Verstoffwechselung von Hämoglobin steigt der Bilirubinspiegel, was zu Gelbsucht führt, einer Erkrankung, die schwerwiegend sein kann. Daher müssen Menschen, die an einem G6PD-Mangel leiden, bestimmte Lebensmittel und Medikamente meiden, die Chemikalien enthalten, die eine Schädigung ihrer roten Blutkörperchen mit Glutathionmangel hervorrufen könnten. Enzymfunktion und -struktur Enzyme werden basierend auf der spezifischen Funktion, die sie erfüllen, in verschiedene Klassen eingeteilt. Beispielsweise sind Oxidoreduktasen an Redoxreaktionen beteiligt, während Transferasen die Übertragung funktioneller Gruppen katalysieren. Die Bindungsbildung bei der ATP-Hydrolyse erfordert Ligasen, wohingegen Hydrolysereaktionen und die Bildung von Doppelbindungen durch Hydrolasen bzw. Lyasen katalysiert werden. Isomeraseenzyme katalysieren normalerweise Isomerisierungsreaktionen. Enzyme besitzen im Allgemeinen aktive Zentren. Hierbei handelt es sich um spezifische Regionen auf dem Molekül mit einer Konformation, die die Bindung des Enzyms an ein bestimmtes Substrat (ein Reaktantenmolekül) begünstigt, um einen Enzym-Substrat-Komplex oder das Reaktionszwischenprodukt zu bilden. Zwei Modelle – das Schlüssel-Schloss-Modell und das induzierte Anpassungsmodell – versuchen, die Funktionsweise eines aktiven Zentrums zu erklären (Abbildung 1). Die einfachste Schloss-und-Schlüssel-Hypothese legt nahe, dass das aktive Zentrum und die Molekülform des Substrats komplementär sind und wie ein Schlüssel in ein Schloss zusammenpassen (Abbildung 1a). Andererseits legt die Hypothese der induzierten Anpassung nahe, dass das Enzymmolekül flexibel ist und seine Form ändert, um eine Bindung mit dem Substrat einzugehen (Abbildung 1b). Sowohl das Schlüssel-Schloss-Modell als auch das induzierte Anpassungsmodell berücksichtigen jedoch die Tatsache, dass Enzyme nur an bestimmte Substrate binden können und nur eine bestimmte Reaktion katalysieren. <img alt="Eq1" src="/files/ftp_upload/11384/11384_Image_1.png" style="text-align: center; height: 300px;"> Abbildung 1 (a) Nach dem Schlüssel-Schloss-Modell passt die Form des aktiven Zentrums eines Enzyms perfekt zum Substrat. (b) Gemäß dem Modell der induzierten Anpassung ist das aktive Zentrum einigermaßen flexibel und kann seine Form ändern, um sich mit dem Substrat zu verbinden. Enzyminhibitoren Die Aktivität von Enzymen kann auch durch den Prozess der Enzymhemmung unterbrochen werden. Es gibt mehrere gängige Arten der Enzymhemmung. Bei der kompetitiven Hemmung bindet ein anderes Molekül (natürlich oder synthetisch) als das Substrat direkt an das aktive Zentrum des Enzyms. Die strukturelle und chemische Ähnlichkeit des Inhibitors mit dem Substrat erleichtert seine Bindung an das aktive Zentrum. Solche kompetitiven Inhibitoren konkurrieren daher mit Substraten und verhindern, dass diese an das Enzym binden. In den meisten Fällen kann eine Erhöhung der Substratkonzentration die Wirkung einer kompetitiven Hemmung unterdrücken. Bei der nichtkompetitiven Hemmung bindet ein Molekül (natürlich oder synthetisch) an eine allosterische (andere) Region des Enzyms, die sich von seinem aktiven Zentrum unterscheidet. Die Bindung des Inhibitors führt zu einer Konformationsänderung des aktiven Zentrums des Enzyms, was zu einer Verringerung der Fähigkeit des Enzyms, die Reaktion zu katalysieren, führt. Im Gegensatz zur kompetitiven Hemmung schwächt eine Erhöhung der Substratkonzentration die hemmenden Wirkungen der nichtkompetitiven Hemmung nicht ab. Dieser Text ist adaptiert von <a href="https://openstax.org/books/chemistry-2e/pages/12-7-catalysis">Openstax, Chemistry 2e, Section 12.7: Catalysis.</a>

Enzyme

Im Inneren lebender Organismen wirken Enzyme als Katalysatoren für viele biochemische Reaktionen, die am Zellstoffwechsel beteiligt sind. Die Rolle von Enzymen besteht darin, die ...

Education

Lehre

JoVE Core

Chemie

Eins

Chemical Kinetics

Chemische Kinetik

KEY TERMS AND CONCEPTS

KERNBEGRIFFE UND KONZEPTE

enzyme action and inhibition

Enzymes are biological catalysts that speed up many reactions in living organisms. They help control cellular metabolism by lowering the activation energy needed for biochemical reactions. When activation energy drops, reaction rates can increase.

Enzyme problems can also lead to serious disease. A genetic abnormality that causes G6PD, or glucose-6-phosphate dehydrogenase, deficiency can disrupt the pathway that supplies NADPH to cells. In red blood cells, this can reduce glutathione and damage other enzymes and proteins such as hemoglobin. As hemoglobin is broken down too much, bilirubin builds up and can cause jaundice. People with G6PD deficiency often need to avoid certain foods and medicines that may trigger damage to their red blood cells.

Enzymes are grouped by the reactions they carry out. Oxidoreductases take part in redox reactions. Transferases move functional groups from one molecule to another. Ligases form bonds and use ATP hydrolysis, while hydrolases drive hydrolysis reactions and lyases help form double bonds. Isomerases catalyze isomerization reactions.

Most enzymes have an active site, which is the region that binds a specific substrate, or reactant molecule. The enzyme and substrate form an enzyme-substrate complex, which acts as the reaction intermediate. Two models explain how this binding works. In the lock-and-key model, the active site and substrate fit together like a key in a lock. In the induced-fit model, the enzyme changes shape to fit the substrate. Both models explain enzyme specificity, meaning an enzyme usually binds only certain substrates and catalyzes only one particular reaction.

Enzyme activity can also be blocked by inhibitors. In competitive inhibition, an inhibitor that is similar to the substrate binds directly to the active site and competes with the substrate. Increasing substrate concentration can often reduce this effect. In non-competitive inhibition, the inhibitor binds to an allosteric site, which is a different region of the enzyme. This binding changes the shape of the active site and lowers enzyme activity. Unlike competitive inhibition, adding more substrate does not fix non-competitive inhibition.

Enzyme Action and Inhibition

reaction rate

Measuring Reaction Rates

Measuring reaction rates shows how fast reactants are used up or products are formed over time. The rate of reaction is the change in the amount of a reactant or product per unit time. Because of that, scientists measure how a property changes as the reaction proceeds and connect that change to reactant or product amounts. For reactions that make or use a gas, the rate can be followed by changes in volume or pressure. A rate expression is the mathematical way to write how concentration changes...

measuring reaction rates

Tracking Reaction Kinetics with Light and Pressure

Reaction kinetics can be tracked with polarimetry, spectrometry, and pressure measurements. These methods let scientists follow a reaction without disturbing the sample. They also help determine how reactant or product concentrations change over time. Polarimetry is used for optically active substances. These substances rotate the plane of polarized light, which is called optical rotation. The effect comes from molecular structure. Normal monochromatic light is unpolarized, but after it passes...

concentration and rate law

Reaction Order from Concentration

Reaction order from concentration shows how reactant amounts affect reaction rate. Rate laws, also called differential rate laws or rate equations, are mathematical expressions that connect reaction rate with the concentrations of reactants. For a generic reaction a A + b B → products, the rate law can be written using the reactant concentrations [A] and [B] and a rate constant k. In a rate law, k is the rate constant for one specific reaction at one specific temperature. The exponents m and n...

determining order of reaction

Finding Rate Law from Initial Rates

Rate laws connect the speed of a chemical reaction to the concentration of its reactants. The rate constant, k, and the reaction orders are not taken from the chemical equation. They are found experimentally by watching how the rate changes when the reactant concentrations change. One common way to do this is the method of initial rates. In this method, several trials are run with different starting concentrations. The measured rates are then compared to determine the reaction orders and,...

the integrated rate law: the dependence of concentration on time

the-integrated-rate-law-the-dependence-of-concentration-on-time

Reading Reaction Progress with Integrated Laws

Integrated rate laws connect reaction concentration to time. They help show how much reactant or product is present after a certain period. They can also help estimate how long a reaction must run to reach a given extent. A common use is finding how long radioactive material must be stored before its radioactivity drops to a safe level. These equations come from the differential rate law after it is integrated with respect to time. For a first-order reaction, where rate = k[A], the integrated...

half-life of a reaction

Reaction Half-Life in Kinetics

Reaction half-life is the time needed for half of a reactant to be consumed. After each half-life, half of the remaining reactant is used up. A hydrogen peroxide decomposition example shows this pattern clearly. The concentration drops from 1.000 M to 0.500 M in the first 6.00 hours, then to 0.250 M in the next 6.00 hours, and then to 0.125 M in the third period. Each later 6.00-hour interval removes half of what is left. For first-order reactions, the half-life does not depend on the reactant...

temperature dependence on reaction rate

Collision Theory and Reaction Speed

Collision theory explains why reaction speed depends on how particles collide. Atoms, molecules, or ions must come close together before they can react. The theory says the reaction rate depends on the collision rate, the orientation of the colliding species, and whether the collision has enough energy for bonds to change. A gas-phase reaction between carbon monoxide and oxygen shows why orientation matters. The molecules can collide in more than one way. If the oxygen side of carbon monoxide...

arrhenius plots

Determining Activation Energy from Temperature

The Arrhenius equation links activation energy and the rate constant, k, for chemical reactions. It is written as k = Ae−Ea/RT. In this equation, R is the ideal gas constant with a value of 8.314 J/mol·K, T is the temperature on the kelvin scale, Ea is the activation energy in J/mole, e is the constant 2.7183, and A is the frequency factor. The frequency factor depends on collision frequency and the orientation of reacting molecules. Experimental kinetic data can be used to find the activation...

reaction mechanisms

Elementary Steps in Reaction Mechanisms

Chemical reactions can happen in steps, and a balanced equation does not show the full path at the molecular level. A reaction mechanism, also called a reaction path, gives the step-by-step process that explains how reactants become products. The decomposition of ozone is one example of a reaction that can be described by a sequence of steps. Each step in a mechanism is an elementary reaction. These elementary reactions happen in order, and when they are added together, they give the balanced...

rate-determining steps

Reaction Bottlenecks in Chemical Kinetics

Reaction bottlenecks help explain rate-determining steps in multistep reaction mechanisms. In a mechanism with several elementary steps, one step is often much slower than the others. That slowest step is called the rate-limiting step, or rate-determining step. A reaction cannot move faster than its slowest step, so this step controls the overall reaction rate. The idea is like traffic on a four-lane freeway with one lane closed. Cars can only move as fast as the bottleneck allows. In the same...

catalysis

Catalyst Action in Reaction Rates

Catalysts change the rate of a chemical reaction by giving it a faster path. A catalyst increases reaction rate without being consumed during the process. Its effect is often explained with reaction mechanisms and energy diagrams. For an endothermic reaction, the reactants and products start and end at the same energies in both cases. The uncatalyzed path is a one-step mechanism with one transition state. The catalyzed path follows a different mechanism with two transition states and a lower...

enzymes

Enzymes are biological catalysts that speed up many reactions in living organisms. They help control cellular metabolism by lowering the activation energy needed for biochemical reactions. When activation energy drops, reaction rates can increase. Enzyme problems can also lead to serious disease. A genetic abnormality that causes G6PD, or glucose-6-phosphate dehydrogenase, deficiency can disrupt the pathway that supplies NADPH to cells. In red blood cells, this can reduce glutathione and...

key terms and concepts

Explore how enzymes speed reactions, how active sites work, and how competitive and non-competitive inhibitors affect enzyme activity in high school biology.

Enzyme Action and Inhibition | JoVE K12

chemistry

JoVE Core Chemie erweckt allgemeine Konzepte der Chemie durch kompakte und leicht verständliche animierte Videolektionen zum Leben. Außerdem zeigen wir in den Videos Wissenschaftler in Aktion bei klassischen und neuartigen Forschungsexperimenten, wie sie heutzutage in Laboren weltweit durchgeführt wurden.

Pennsylvania State Academic Standards

Physical Science

Chemical Reactions

3.2.9-12.D

3.2.9-12.E

ohios-learning-standards-and-model-curriculum

Ohio’s Learning Standards and Model Curriculum

Interactions Of Matter

Chemical reactions

Virginia  Standards of Learning

HIgh School

CH.7

CH.7.f

Arizona Science Standards

High School

HS.P1

HS.P1U1.3

Next Generation Science Standards

Matter and Its Interactions

HS-PS1-4

HS-PS1-5

Florida Department of Education

SC.912.P.12

SC.912.P.12.12

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Use models to explain how the scientific understanding of atomic structure has evolved.

PS.Chm.1.1

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Nuclear Power

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Use models to compare nuclear reactions including alpha decay, beta decay and gamma decay; nuclear fusion and nuclear fission.

PS.Chm.1.2

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The Energies of Atomic Orbitals

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PS.Chm.1.3

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Molar Mass

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PS.Chm.2.1

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Ionic Radii

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Construct an explanation to infer the atomic size, reactivity, electronegativity, and ionization energy of an element based on its position in the Periodic Table.

PS.Chm.2.2

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The Born-Haber Cycle

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Resonance

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	...

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Analyze and interpret data to explain the mechanisms and properties of the two main types of intramolecular (ionic and covalent) bonds.

PS.Chm.3.1

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Intermolecular vs Intramolecular Forces

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Comparing Intermolecular Forces: Melting Point, Boiling Point, and Miscibility

Intermolecular forces are attractive forces that exist between molecules. They dictate several bulk properties, such as melting points, boiling points, ...

Construct an explanation to summarize the influences intermolecular forces have on the properties of chemical compounds.

PS.Chm.3.2

Analyze the structure of atoms and isotopes.

Enzyme Action and Inhibition

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