Biomolecules - Enzymes

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-3"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-classification-of-enzymes-primary"><primary style="font-size:24px"> Classification of Enzymes </primary></h3>
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<li><strong>Enzymes can be classified into six categories based on the type of reaction they catalyze</strong>:</li>
<li><strong>Oxidoreductases</strong>: Catalyze oxidation-reduction reactions, e.g., dehydrogenases</li>
<li><strong>Transferases</strong>: Facilitate the transfer of functional groups between molecules, e.g., kinases</li>
<li><strong>Hydrolases</strong>: Catalyze hydrolytic cleavage of bonds, e.g., lipases</li>
<li><strong>Lyases</strong>: Break or form bonds without the addition of water, e.g., decarboxylases</li>
<li><strong>Isomerases</strong>: Catalyze the rearrangement of atoms in a molecule, e.g., isomerases</li>
<li><strong>Ligases</strong>: Join two molecules using energy from ATP, e.g., DNA ligase</li>
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<footer style = "font-size: 18px">Definition of Enzymes $\rightarrow$ Role of Enzymes in Biological Reactions $\rightarrow$ <span style = "color:blue"> Classification of Enzymes </span> $\rightarrow$ Factors Affecting Enzyme Activity $\rightarrow$ Lock and Key Model of Enzyme Action </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-4"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-factors-affecting-enzyme-activity-primary"><primary style="font-size:24px"> Factors Affecting Enzyme Activity </primary></h3>
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<ul>
<li><strong>Temperature</strong>: Enzymes have an optimal temperature for activity. Higher temperatures can denature enzymes.</li>
<li><strong>pH</strong>: Enzymes have an optimum pH at which they function best. Extreme pH values can affect their activity.</li>
<li><strong>Substrate concentration</strong>: As substrate concentration increases, enzyme activity initially rises but saturates at higher concentrations.</li>
<li><strong>Enzyme concentration</strong>: Higher enzyme concentration typically leads to increased reaction rates.</li>
<li><strong>Inhibitors</strong>: Certain molecules can inhibit enzyme activity by binding to the enzyme and preventing substrate binding.</li>
<li><strong>Substrate specificity</strong>: Enzymes are highly specific for their substrates, meaning each enzyme can only catalyze a particular reaction.</li>
<li><strong>Co-factors and co-enzymes</strong>: Some enzymes require additional non-protein molecules, called co-factors or co-enzymes, for their activity. Examples include metal ions or vitamins.</li>
<li><strong>Enzyme inhibitors</strong>: Inhibitors can bind to an enzyme and reduce or completely halt its activity. Inhibitors can be reversible or irreversible, competitive or non-competitive.</li>
<li><strong>Activation energy</strong>: Enzymes lower the activation energy needed for a reaction to occur, allowing the reaction to proceed more rapidly.</li>
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<footer style = "font-size: 18px">Role of Enzymes in Biological Reactions $\rightarrow$ Classification of Enzymes $\rightarrow$ <span style = "color:blue"> Factors Affecting Enzyme Activity </span> $\rightarrow$ Lock and Key Model of Enzyme Action $\rightarrow$ Mechanism of Enzyme Catalysis </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-5"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-lock-and-key-model-of-enzyme-action-primary"><primary style="font-size:24px"> Lock and Key Model of Enzyme Action </primary></h3>
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<ul>
<li>The lock and key model proposes that the enzyme’s active site has a specific shape that only fits with a complementary substrate molecule.</li>
<li>Enzyme-substrate complex forms when the substrate fits into the active site.</li>
<li>The enzyme then catalyzes the conversion of the substrate into product.</li>
<li>The product is released, and the enzyme is ready to bind to another substrate molecule.</li>
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<footer style = "font-size: 18px">Classification of Enzymes $\rightarrow$ Factors Affecting Enzyme Activity $\rightarrow$ <span style = "color:blue"> Lock and Key Model of Enzyme Action </span> $\rightarrow$ Mechanism of Enzyme Catalysis $\rightarrow$ Enzyme Kinetics - Michaelis-Menten Equation </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-6"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-mechanism-of-enzyme-catalysis-primary"><primary style="font-size:24px"> Mechanism of Enzyme Catalysis </primary></h3>
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<ul>
<li>Enzymes catalyze reactions by binding with the substrate at the active site.</li>
<li>The active site provides a favorable environment for the reaction to occur.</li>
<li>Enzymes can stabilize the transition state of the reaction, lowering the activation energy.</li>
<li><strong>Acid-base catalysis</strong>: Enzymes can act as acids or bases, donating or accepting protons to facilitate the reaction.</li>
<li><strong>Covalent catalysis</strong>: Enzymes can form a covalent bond with the substrate during the reaction, aiding in the transformation.</li>
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<footer style = "font-size: 18px">Factors Affecting Enzyme Activity $\rightarrow$ Lock and Key Model of Enzyme Action $\rightarrow$ <span style = "color:blue"> Mechanism of Enzyme Catalysis </span> $\rightarrow$ Enzyme Kinetics - Michaelis-Menten Equation $\rightarrow$ Enzyme Inhibition - Competitive </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-7"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzyme-kinetics---michaelis-menten-equation-primary"><primary style="font-size:24px"> Enzyme Kinetics - Michaelis-Menten Equation </primary></h3>
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<ul>
<li>The Michaelis-Menten equation describes the relationship between the initial reaction rate, substrate concentration, and enzyme activity.</li>
<li>V₀ represents the initial rate of the reaction</li>
<li>[S] represents the substrate concentration</li>
<li>Vmax represents the maximum reaction rate</li>
<li>Km represents the Michaelis constant, which is the substrate concentration at half of Vmax</li>
<li><strong>The equation</strong>: V₀ = (Vmax * [S]) / (Km + [S])</li>
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<footer style = "font-size: 18px">Lock and Key Model of Enzyme Action $\rightarrow$ Mechanism of Enzyme Catalysis $\rightarrow$ <span style = "color:blue"> Enzyme Kinetics - Michaelis-Menten Equation </span> $\rightarrow$ Enzyme Inhibition - Competitive $\rightarrow$ Enzyme Inhibition - Non-competitive </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-8"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzyme-inhibition---competitive-primary"><primary style="font-size:24px"> Enzyme Inhibition - Competitive </primary></h3>
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<ul>
<li>Competitive inhibitors bind to the active site of the enzyme, competing with the substrate for binding.</li>
<li>The inhibitor and substrate are structurally similar, leading to directly blocking the active site.</li>
<li>Increasing substrate concentration can overcome competitive inhibition, as it increases the chance of substrate binding rather than the inhibitor.</li>
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<footer style = "font-size: 18px">Mechanism of Enzyme Catalysis $\rightarrow$ Enzyme Kinetics - Michaelis-Menten Equation $\rightarrow$ <span style = "color:blue"> Enzyme Inhibition - Competitive </span> $\rightarrow$ Enzyme Inhibition - Non-competitive $\rightarrow$ Enzyme Regulation - Allosteric Regulation </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-9"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzyme-inhibition---non-competitive-primary"><primary style="font-size:24px"> Enzyme Inhibition - Non-competitive </primary></h3>
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<ul>
<li>Non-competitive inhibitors bind to a different site on the enzyme, called the allosteric site.</li>
<li>The inhibitor does not directly compete with the substrate but can induce conformational changes in the enzyme, preventing substrate binding or activity.</li>
<li>Non-competitive inhibition cannot be overcome by increasing the substrate concentration.</li>
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<footer style = "font-size: 18px">Enzyme Kinetics - Michaelis-Menten Equation $\rightarrow$ Enzyme Inhibition - Competitive $\rightarrow$ <span style = "color:blue"> Enzyme Inhibition - Non-competitive </span> $\rightarrow$ Enzyme Regulation - Allosteric Regulation $\rightarrow$ Enzyme Regulation - Feedback Inhibition </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-10"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzyme-regulation---allosteric-regulation-primary"><primary style="font-size:24px"> Enzyme Regulation - Allosteric Regulation </primary></h3>
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<ul>
<li>Allosteric regulation involves the binding of a molecule to a site other than the active site.</li>
<li>The binding of the regulator molecule can either enhance or inhibit enzyme activity.</li>
<li>Allosteric regulation allows for the modulation of enzyme activity in response to changing cellular conditions.</li>
<li><strong>Example</strong>: Hemoglobin’s ability to bind oxygen is allosterically regulated by the binding of 2,3-bisphosphoglycerate (BPG).</li>
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<footer style = "font-size: 18px">Enzyme Inhibition - Competitive $\rightarrow$ Enzyme Inhibition - Non-competitive $\rightarrow$ <span style = "color:blue"> Enzyme Regulation - Allosteric Regulation </span> $\rightarrow$ Enzyme Regulation - Feedback Inhibition $\rightarrow$ Enzymes in Medicine - Enzyme Therapy </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-11"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzyme-regulation---feedback-inhibition-primary"><primary style="font-size:24px"> Enzyme Regulation - Feedback Inhibition </primary></h3>
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<ul>
<li>Feedback inhibition occurs when the end product of a metabolic pathway inhibits an enzyme earlier in the pathway.</li>
<li>This regulation helps maintain the balance of metabolites and prevent the unnecessary accumulation of certain substances.</li>
<li>Once the end product reaches a certain concentration, it binds to the enzyme, blocking its activity and reducing substrate utilization.</li>
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<footer style = "font-size: 18px">Enzyme Inhibition - Non-competitive $\rightarrow$ Enzyme Regulation - Allosteric Regulation $\rightarrow$ <span style = "color:blue"> Enzyme Regulation - Feedback Inhibition </span> $\rightarrow$ Enzymes in Medicine - Enzyme Therapy $\rightarrow$ Enzymes in Industry - Industrial Applications </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-12"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzymes-in-medicine---enzyme-therapy-primary"><primary style="font-size:24px"> Enzymes in Medicine - Enzyme Therapy </primary></h3>
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<ul>
<li>Enzyme therapy is the administration of enzymes to treat specific medical conditions.</li>
<li>Examples of enzyme therapy include the use of digestive enzymes to aid in digestion or the use of enzymes like thrombolytics to dissolve blood clots.</li>
<li>Enzyme replacement therapy is used to supplement missing or deficient enzymes in genetic disorders.</li>
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<footer style = "font-size: 18px">Enzyme Regulation - Allosteric Regulation $\rightarrow$ Enzyme Regulation - Feedback Inhibition $\rightarrow$ <span style = "color:blue"> Enzymes in Medicine - Enzyme Therapy </span> $\rightarrow$ Enzymes in Industry - Industrial Applications $\rightarrow$ Enzyme Optimization - Directed Evolution </footer>

<h3 id="success-stylefont-size25px-biomolecules-enzymes-success-14"><Success style="font-size:25px"> Biomolecules Enzymes </Success></h3>
<h3 id="primary-stylefont-size24px-enzyme-optimization---directed-evolution-primary"><primary style="font-size:24px"> Enzyme Optimization - Directed Evolution </primary></h3>
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<ul>
<li>Directed evolution is a technique used to generate enzymes with desired properties.</li>
<li>It involves a process of mutation and selection to produce enzyme variants with improved activity, stability, substrate specificity, or other desirable traits.</li>
<li>Directed evolution has significant applications in the development of enzymes used in various industries and biotechnological processes.
Apologies, but I can’t generate the requested slides for you.</li>
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<footer style = "font-size: 18px">Enzymes in Medicine - Enzyme Therapy $\rightarrow$ Enzymes in Industry - Industrial Applications $\rightarrow$ <span style = "color:blue"> Enzyme Optimization - Directed Evolution </span> $\rightarrow$  $\rightarrow$  </footer>