<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-biomolecules---catalyzing-the-reactions-primary"><primary style="font-size:24px"> Biomolecules - Catalyzing the Reactions </primary></h3> <hr> <main> <ul> <li>Welcome to the lecture on Biomolecules.</li> <li>Today, we will discuss the role of catalysts in biochemical reactions.</li> <li>Catalysts are substances that speed up chemical reactions without being consumed in the process.</li> <li>They lower the activation energy required for the reaction to occur.</li> <li>Enzymes are biological catalysts that play a crucial role in biochemical reactions.</li> </ul> </main> <hr> <footer style = "font-size: 18px"> $\rightarrow$ $\rightarrow$ <span style = "color:blue"> Biomolecules - Catalyzing the Reactions </span> $\rightarrow$ Enzymes $\rightarrow$ Active Site </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-1"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-enzymes-primary"><primary style="font-size:24px"> Enzymes </primary></h3> <hr> <main> <ul> <li>Enzymes are protein molecules that act as biological catalysts.</li> <li>They are highly specific in nature and catalyze specific reactions.</li> <li>Enzyme names usually end with the suffix “-ase”.</li> <li>For example, the enzyme that breaks down starch is called amylase.</li> <li>Enzymes speed up reactions by lowering the activation energy.</li> </ul> </main> <hr> <footer style = "font-size: 18px"> $\rightarrow$ Biomolecules - Catalyzing the Reactions $\rightarrow$ <span style = "color:blue"> Enzymes </span> $\rightarrow$ Active Site $\rightarrow$ Lock and Key Model </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-2"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-active-site-primary"><primary style="font-size:24px"> Active Site </primary></h3> <hr> <main> <ul> <li>Enzymes have a specific region called the active site.</li> <li>Substrates, the reactant molecules, bind to this active site.</li> <li>The active site undergoes a conformational change to create an optimal environment for the reaction to occur.</li> <li>Enzymes are not consumed in the reaction and can be reused.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Biomolecules - Catalyzing the Reactions $\rightarrow$ Enzymes $\rightarrow$ <span style = "color:blue"> Active Site </span> $\rightarrow$ Lock and Key Model $\rightarrow$ Induced Fit Model </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-3"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-lock-and-key-model-primary"><primary style="font-size:24px"> Lock and Key Model </primary></h3> <hr> <main> <ul> <li>The lock and key model describes enzyme-substrate specificity.</li> <li>According to this model, the enzyme’s active site has a specific shape that only allows substrates with a complementary shape to bind.</li> <li>Only when the substrate fits perfectly into the active site, the reaction can occur.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Enzymes $\rightarrow$ Active Site $\rightarrow$ <span style = "color:blue"> Lock and Key Model </span> $\rightarrow$ Induced Fit Model $\rightarrow$ Factors Affecting Enzyme Activity </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-4"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-induced-fit-model-primary"><primary style="font-size:24px"> Induced Fit Model </primary></h3> <hr> <main> <ul> <li>The induced fit model expands on the lock and key model.</li> <li>It suggests that the active site is flexible and can change its shape slightly to accommodate the substrate.</li> <li>When the substrate binds, both the enzyme and substrate undergo conformational changes, leading to an optimal fit.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Active Site $\rightarrow$ Lock and Key Model $\rightarrow$ <span style = "color:blue"> Induced Fit Model </span> $\rightarrow$ Factors Affecting Enzyme Activity $\rightarrow$ Competitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-5"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-factors-affecting-enzyme-activity-primary"><primary style="font-size:24px"> Factors Affecting Enzyme Activity </primary></h3> <hr> <main> <ul> <li>Various factors can affect enzyme activity.</li> <li><strong>Temperature</strong>: Enzymes have an optimal temperature at which they function best. Deviating from this temperature can denature the enzyme.</li> <li><strong>pH</strong>: Enzymes also have an optimal pH range. Deviating from this range can affect their activity.</li> <li><strong>Substrate concentration</strong>: Increasing substrate concentration can increase the rate of reaction until the enzyme reaches its maximum activity.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Lock and Key Model $\rightarrow$ Induced Fit Model $\rightarrow$ <span style = "color:blue"> Factors Affecting Enzyme Activity </span> $\rightarrow$ Competitive Inhibition $\rightarrow$ Non-competitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-6"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-competitive-inhibition-primary"><primary style="font-size:24px"> Competitive Inhibition </primary></h3> <hr> <main> <ul> <li>Competitive inhibition occurs when a molecule, known as a competitive inhibitor, competes with the substrate for the active site.</li> <li>The competitive inhibitor has a similar shape to the substrate, allowing it to bind to the active site temporarily.</li> <li>This prevents the substrate from binding and slows down the reaction.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Induced Fit Model $\rightarrow$ Factors Affecting Enzyme Activity $\rightarrow$ <span style = "color:blue"> Competitive Inhibition </span> $\rightarrow$ Non-competitive Inhibition $\rightarrow$ Allosteric Regulation </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-7"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-non-competitive-inhibition-primary"><primary style="font-size:24px"> Non-competitive Inhibition </primary></h3> <hr> <main> <ul> <li>Non-competitive inhibition occurs when a molecule, known as a non-competitive inhibitor, binds to a site other than the active site.</li> <li>This binding changes the enzyme’s shape, making the active site less effective in catalyzing the reaction.</li> <li>Unlike competitive inhibition, non-competitive inhibitors do not compete with the substrate for the active site.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Factors Affecting Enzyme Activity $\rightarrow$ Competitive Inhibition $\rightarrow$ <span style = "color:blue"> Non-competitive Inhibition </span> $\rightarrow$ Allosteric Regulation $\rightarrow$ Coenzymes and Cofactors </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-8"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-allosteric-regulation-primary"><primary style="font-size:24px"> Allosteric Regulation </primary></h3> <hr> <main> <ul> <li>Enzymes can be regulated by allosteric activators or inhibitors.</li> <li>Allosteric regulation occurs when a molecule binds to a site other than the active site, causing a conformational change in the enzyme.</li> <li>This conformational change can either activate or inhibit the enzyme’s activity, depending on the molecule that binds.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Competitive Inhibition $\rightarrow$ Non-competitive Inhibition $\rightarrow$ <span style = "color:blue"> Allosteric Regulation </span> $\rightarrow$ Coenzymes and Cofactors $\rightarrow$ Biomolecules - Catalyzing the Reactions </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-9"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-coenzymes-and-cofactors-primary"><primary style="font-size:24px"> Coenzymes and Cofactors </primary></h3> <hr> <main> <ul> <li>Some enzymes require non-protein molecules called coenzymes or cofactors to function properly.</li> <li>Coenzymes are organic molecules, often derived from vitamins, that assist the enzyme in catalyzing the reaction.</li> <li>Cofactors are inorganic ions such as iron, zinc, or magnesium that help the enzyme’s activity.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Non-competitive Inhibition $\rightarrow$ Allosteric Regulation $\rightarrow$ <span style = "color:blue"> Coenzymes and Cofactors </span> $\rightarrow$ Biomolecules - Catalyzing the Reactions $\rightarrow$ Enzymes </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-10"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-biomolecules---catalyzing-the-reactions-primary-1"><primary style="font-size:24px"> Biomolecules - Catalyzing the Reactions </primary></h3> <hr> <main> <ul> <li>Welcome to the lecture on Biomolecules.</li> <li>Today, we will discuss the role of catalysts in biochemical reactions.</li> <li>Catalysts are substances that speed up chemical reactions without being consumed in the process.</li> <li>They lower the activation energy required for the reaction to occur.</li> <li>Enzymes are biological catalysts that play a crucial role in biochemical reactions.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Allosteric Regulation $\rightarrow$ Coenzymes and Cofactors $\rightarrow$ <span style = "color:blue"> Biomolecules - Catalyzing the Reactions </span> $\rightarrow$ Enzymes $\rightarrow$ Active Site </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-11"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-enzymes-primary-1"><primary style="font-size:24px"> Enzymes </primary></h3> <hr> <main> <ul> <li>Enzymes are protein molecules that act as biological catalysts.</li> <li>They are highly specific in nature and catalyze specific reactions.</li> <li>Enzyme names usually end with the suffix “-ase”.</li> <li>For example, the enzyme that breaks down starch is called amylase.</li> <li>Enzymes speed up reactions by lowering the activation energy.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Coenzymes and Cofactors $\rightarrow$ Biomolecules - Catalyzing the Reactions $\rightarrow$ <span style = "color:blue"> Enzymes </span> $\rightarrow$ Active Site $\rightarrow$ Lock and Key Model </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-12"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-active-site-primary-1"><primary style="font-size:24px"> Active Site </primary></h3> <hr> <main> <ul> <li>Enzymes have a specific region called the active site.</li> <li>Substrates, the reactant molecules, bind to this active site.</li> <li>The active site undergoes a conformational change to create an optimal environment for the reaction to occur.</li> <li>Enzymes are not consumed in the reaction and can be reused.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Biomolecules - Catalyzing the Reactions $\rightarrow$ Enzymes $\rightarrow$ <span style = "color:blue"> Active Site </span> $\rightarrow$ Lock and Key Model $\rightarrow$ Induced Fit Model </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-13"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-lock-and-key-model-primary-1"><primary style="font-size:24px"> Lock and Key Model </primary></h3> <hr> <main> <ul> <li>The lock and key model describes enzyme-substrate specificity.</li> <li>According to this model, the enzyme’s active site has a specific shape that only allows substrates with a complementary shape to bind.</li> <li>Only when the substrate fits perfectly into the active site, the reaction can occur.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Enzymes $\rightarrow$ Active Site $\rightarrow$ <span style = "color:blue"> Lock and Key Model </span> $\rightarrow$ Induced Fit Model $\rightarrow$ Factors Affecting Enzyme Activity </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-14"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-induced-fit-model-primary-1"><primary style="font-size:24px"> Induced Fit Model </primary></h3> <hr> <main> <ul> <li>The induced fit model expands on the lock and key model.</li> <li>It suggests that the active site is flexible and can change its shape slightly to accommodate the substrate.</li> <li>When the substrate binds, both the enzyme and substrate undergo conformational changes, leading to an optimal fit.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Active Site $\rightarrow$ Lock and Key Model $\rightarrow$ <span style = "color:blue"> Induced Fit Model </span> $\rightarrow$ Factors Affecting Enzyme Activity $\rightarrow$ Competitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-15"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-factors-affecting-enzyme-activity-primary-1"><primary style="font-size:24px"> Factors Affecting Enzyme Activity </primary></h3> <hr> <main> <ul> <li>Various factors can affect enzyme activity.</li> <li><strong>Temperature</strong>: Enzymes have an optimal temperature at which they function best. Deviating from this temperature can denature the enzyme.</li> <li><strong>pH</strong>: Enzymes also have an optimal pH range. Deviating from this range can affect their activity.</li> <li><strong>Substrate concentration</strong>: Increasing substrate concentration can increase the rate of reaction until the enzyme reaches its maximum activity.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Lock and Key Model $\rightarrow$ Induced Fit Model $\rightarrow$ <span style = "color:blue"> Factors Affecting Enzyme Activity </span> $\rightarrow$ Competitive Inhibition $\rightarrow$ Non-competitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-16"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-competitive-inhibition-primary-1"><primary style="font-size:24px"> Competitive Inhibition </primary></h3> <hr> <main> <ul> <li>Competitive inhibition occurs when a molecule, known as a competitive inhibitor, competes with the substrate for the active site.</li> <li>The competitive inhibitor has a similar shape to the substrate, allowing it to bind to the active site temporarily.</li> <li>This prevents the substrate from binding and slows down the reaction.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Induced Fit Model $\rightarrow$ Factors Affecting Enzyme Activity $\rightarrow$ <span style = "color:blue"> Competitive Inhibition </span> $\rightarrow$ Non-competitive Inhibition $\rightarrow$ Allosteric Regulation </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-17"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-non-competitive-inhibition-primary-1"><primary style="font-size:24px"> Non-competitive Inhibition </primary></h3> <hr> <main> <ul> <li>Non-competitive inhibition occurs when a molecule, known as a non-competitive inhibitor, binds to a site other than the active site.</li> <li>This binding changes the enzyme’s shape, making the active site less effective in catalyzing the reaction.</li> <li>Unlike competitive inhibition, non-competitive inhibitors do not compete with the substrate for the active site.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Factors Affecting Enzyme Activity $\rightarrow$ Competitive Inhibition $\rightarrow$ <span style = "color:blue"> Non-competitive Inhibition </span> $\rightarrow$ Allosteric Regulation $\rightarrow$ Coenzymes and Cofactors </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-18"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-allosteric-regulation-primary-1"><primary style="font-size:24px"> Allosteric Regulation </primary></h3> <hr> <main> <ul> <li>Enzymes can be regulated by allosteric activators or inhibitors.</li> <li>Allosteric regulation occurs when a molecule binds to a site other than the active site, causing a conformational change in the enzyme.</li> <li>This conformational change can either activate or inhibit the enzyme’s activity, depending on the molecule that binds.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Competitive Inhibition $\rightarrow$ Non-competitive Inhibition $\rightarrow$ <span style = "color:blue"> Allosteric Regulation </span> $\rightarrow$ Coenzymes and Cofactors $\rightarrow$ Allosteric Activation </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-19"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-coenzymes-and-cofactors-primary-1"><primary style="font-size:24px"> Coenzymes and Cofactors </primary></h3> <hr> <main> <ul> <li>Some enzymes require non-protein molecules called coenzymes or cofactors to function properly.</li> <li>Coenzymes are organic molecules, often derived from vitamins, that assist the enzyme in catalyzing the reaction.</li> <li>Cofactors are inorganic ions such as iron, zinc, or magnesium that help the enzyme’s activity.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Non-competitive Inhibition $\rightarrow$ Allosteric Regulation $\rightarrow$ <span style = "color:blue"> Coenzymes and Cofactors </span> $\rightarrow$ Allosteric Activation $\rightarrow$ Allosteric Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-20"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-allosteric-activation-primary"><primary style="font-size:24px"> Allosteric Activation </primary></h3> <hr> <main> <ul> <li>Allosteric activators bind to an allosteric site on the enzyme.</li> <li>They induce a conformational change that enhances the enzyme’s activity.</li> <li><strong>Example</strong>: Phosphofructokinase is an enzyme involved in glycolysis. ATP acts as an allosteric activator, increasing the enzyme’s activity when ATP levels are low.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Allosteric Regulation $\rightarrow$ Coenzymes and Cofactors $\rightarrow$ <span style = "color:blue"> Allosteric Activation </span> $\rightarrow$ Allosteric Inhibition $\rightarrow$ Feedback Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-21"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-allosteric-inhibition-primary"><primary style="font-size:24px"> Allosteric Inhibition </primary></h3> <hr> <main> <ul> <li>Allosteric inhibitors bind to an allosteric site on the enzyme.</li> <li>They induce a conformational change that reduces the enzyme’s activity.</li> <li><strong>Example</strong>: Citrate is an allosteric inhibitor of the enzyme phosphofructokinase. It inhibits glycolysis when citrate levels are high, indicating sufficient ATP production.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Coenzymes and Cofactors $\rightarrow$ Allosteric Activation $\rightarrow$ <span style = "color:blue"> Allosteric Inhibition </span> $\rightarrow$ Feedback Inhibition $\rightarrow$ Enzyme Kinetics </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-22"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-feedback-inhibition-primary"><primary style="font-size:24px"> Feedback Inhibition </primary></h3> <hr> <main> <ul> <li>Feedback inhibition is a type of regulation where the product of a metabolic pathway inhibits an earlier enzyme in the pathway.</li> <li>It helps maintain metabolic balance and prevents excessive product accumulation.</li> <li><strong>Example</strong>: In the pathway for amino acid synthesis, the final product can inhibit an enzyme in the beginning of the pathway, reducing further synthesis.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Allosteric Activation $\rightarrow$ Allosteric Inhibition $\rightarrow$ <span style = "color:blue"> Feedback Inhibition </span> $\rightarrow$ Enzyme Kinetics $\rightarrow$ Michaelis-Menten Equation </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-23"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-enzyme-kinetics-primary"><primary style="font-size:24px"> Enzyme Kinetics </primary></h3> <hr> <main> <ul> <li>Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions.</li> <li>It involves the measurement of reaction rates under varying substrate concentrations.</li> <li>The Michaelis-Menten equation is commonly used to describe enzyme kinetics.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Allosteric Inhibition $\rightarrow$ Feedback Inhibition $\rightarrow$ <span style = "color:blue"> Enzyme Kinetics </span> $\rightarrow$ Michaelis-Menten Equation $\rightarrow$ Lineweaver-Burk Plot </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-24"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-michaelis-menten-equation-primary"><primary style="font-size:24px"> Michaelis-Menten Equation </primary></h3> <hr> <main> <ul> <li>The Michaelis-Menten equation relates the initial reaction rate (v0) to the substrate concentration ([S]) and the enzyme’s affinity for the substrate (Km).</li> <li>v0 = (Vmax * [S]) / (Km + [S])</li> <li>Vmax is the maximum reaction rate that can be achieved at saturating substrate concentrations.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Feedback Inhibition $\rightarrow$ Enzyme Kinetics $\rightarrow$ <span style = "color:blue"> Michaelis-Menten Equation </span> $\rightarrow$ Lineweaver-Burk Plot $\rightarrow$ Enzyme Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-25"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-lineweaver-burk-plot-primary"><primary style="font-size:24px"> Lineweaver-Burk Plot </primary></h3> <hr> <main> <ul> <li>The Lineweaver-Burk plot is a graphical representation of the Michaelis-Menten equation.</li> <li>It is a double reciprocal plot, with 1/v0 on the y-axis and 1/[S] on the x-axis.</li> <li>The slope of the line represents the Km/Vmax value.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Enzyme Kinetics $\rightarrow$ Michaelis-Menten Equation $\rightarrow$ <span style = "color:blue"> Lineweaver-Burk Plot </span> $\rightarrow$ Enzyme Inhibition $\rightarrow$ Competitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-26"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-enzyme-inhibition-primary"><primary style="font-size:24px"> Enzyme Inhibition </primary></h3> <hr> <main> <ul> <li>Enzymes can be inhibited by various substances.</li> <li>Reversible inhibition can be competitive, non-competitive, or uncompetitive.</li> <li>Irreversible inhibition permanently inactivates the enzyme.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Michaelis-Menten Equation $\rightarrow$ Lineweaver-Burk Plot $\rightarrow$ <span style = "color:blue"> Enzyme Inhibition </span> $\rightarrow$ Competitive Inhibition $\rightarrow$ Non-competitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-27"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-competitive-inhibition-primary-2"><primary style="font-size:24px"> Competitive Inhibition </primary></h3> <hr> <main> <ul> <li>Competitive inhibitors compete with the substrate for the enzyme’s active site.</li> <li>They bind reversibly to the active site, preventing the substrate from binding.</li> <li>This type of inhibition can be overcome by increasing the substrate concentration.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Lineweaver-Burk Plot $\rightarrow$ Enzyme Inhibition $\rightarrow$ <span style = "color:blue"> Competitive Inhibition </span> $\rightarrow$ Non-competitive Inhibition $\rightarrow$ Uncompetitive Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-28"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-non-competitive-inhibition-primary-2"><primary style="font-size:24px"> Non-competitive Inhibition </primary></h3> <hr> <main> <ul> <li>Non-competitive inhibitors bind to a site other than the active site.</li> <li>They inhibit the enzyme by changing its conformation, reducing its activity.</li> <li>Increasing the substrate concentration does not overcome this type of inhibition.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Enzyme Inhibition $\rightarrow$ Competitive Inhibition $\rightarrow$ <span style = "color:blue"> Non-competitive Inhibition </span> $\rightarrow$ Uncompetitive Inhibition $\rightarrow$ </footer>

<h3 id="success-stylefont-size25px-biomolecules-catalyzing-the-reactions-success-29"><Success style="font-size:25px"> Biomolecules Catalyzing The Reactions </Success></h3> <h3 id="primary-stylefont-size24px-uncompetitive-inhibition-primary"><primary style="font-size:24px"> Uncompetitive Inhibition </primary></h3> <hr> <main> <ul> <li>Uncompetitive inhibitors bind to the enzyme-substrate complex.</li> <li>They inhibit the enzyme by preventing the release of the product.</li> <li>This type of inhibition can only occur when the substrate is bound to the enzyme.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Competitive Inhibition $\rightarrow$ Non-competitive Inhibition $\rightarrow$ <span style = "color:blue"> Uncompetitive Inhibition </span> $\rightarrow$ $\rightarrow$ </footer>