<div> <h3 id="successbiomolecules-lecture---10success"><Success>Biomolecules (lecture - 10)</Success></h3> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-014-0027.6.jpg"></p> </div>

<div> <h3 id="successenzymessuccess"><Success>Enzymes</Success></h3> </div> <div style='float: left; width:100%;font-size:30px;text-align:left'> <ul> <li>Essentially all organic reaction that occur in cells require a catalyst</li> <li>Most biological catalyst are enzymes, which are globular protien</li> <li>Each biological reaction is catalyzed by a different enzyme</li> <li>Substrate $\xrightarrow{\text { enzyme }}$ Product</li> <li>The enzyme binds its substrate at its active site, a pocket in the cleft of the enzyme</li> </ul> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-016-0086.4.jpg"></p> </div>

<div> <h3 id="successenzymessuccess-1"><Success>Enzymes</Success></h3> </div> <div style='float: left; width:50%;font-size:30px;text-align:left'> <ul> <li>The substrate is bound at the active site</li> <li>The specificity of an enzyme results from its conformation and the particular amino acid side chains that are at the active site</li> </ul> </div> <div style='float: right; width:50%;'> <img src="https://imagedelivery.net/YfdZ0yYuJi8R0IouXWrMsA/4774d211-db89-4a2a-614e-a9c045cea900/public" width="80%"> <!----> </div>

<div> <h3 id="successenzymessuccess-2"><Success>Enzymes</Success></h3> </div> <div style='float: left; width:100%;font-size:30px;text-align:left'> <p><strong>For example -</strong></p> <ul> <li>An amino acid with a negatively charged side chain at the active site can bind with a substrate which has a positively charged group</li> <li>Hydrogen bond donor active site ${-}$ hydrogen bond acceptor and a hydrophobic amino acid side chain can associate with hydrophobic groups on the substrate</li> <li>Emil Fischer proposed the lock-and-key model to account for the specificity of an enzyme for its substrate</li> </ul> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-100-0639.6.jpg"></p> </div>

<div> <h3 id="successenzymessuccess-3"><Success>Enzymes</Success></h3> </div> <div style='float: left; width:50%;font-size:30px;text-align:left'> <ul> <li><strong>Lock- key- model</strong></li> </ul> <ul> <li>1894- Emil fischer</li> </ul> <ul> <li><strong>Induced fit model</strong></li> </ul> <ul> <li>In 1958 Daniel koshland</li> </ul> </div> <div style='float: right; width:50%;'> <img src="https://imagedelivery.net/YfdZ0yYuJi8R0IouXWrMsA/c4f8c6f5-6d67-4650-6b76-0aa2b7f33500/public" width="80%"> <!----> </div>

<div> <h3 id="successcatalyzing-the-reactionsuccess"><Success>Catalyzing the reaction</Success></h3> </div> <div style='float: left; width:100%;font-size:30px;text-align:left'> <ul> <li>Some of the amino acid side chain of the enzyme serves as acid, base, and nucleophilic catalyst and many enzymes have metal ions at their active site that act as catalysts</li> <li>This factor is analogous to the way intramolecular catalyst by acids, bases, nucleophilics and metal ions</li> </ul> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-181-1291.2.jpg"></p> </div>

<div> <h3 id="successcatalyzing-the-reactionsuccess-1"><Success>Catalyzing the reaction</Success></h3> </div> <div style='float: left; width:100%;font-size:30px;text-align:left'> <ul> <li>An acid catalyst increases the rate of a reaction by donating a proton to the substrate</li> <li>A base catalyst increases the rate of a reaction by removing a proton from the substrate</li> <li>A nucleophile catalyst increase the rate of a reaction by forming a covalent bond with the substrate</li> <li>Amino acid side chain can stabilize transition state by london dispersion forces, electrostatic interaction, and hydrogen bonding</li> </ul> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-232-1706.4.jpg"></p> </div>

<div> <h3 id="successcatalyzing-the-reactionsuccess-2"><Success>Catalyzing the reaction</Success></h3> </div> <div style='float: left; width:100%;font-size:30px;text-align:left'> <ul> <li>Enzymes are generally named after the compound or class of compound upon which they work</li> <li><strong>Example -</strong> the enzyme that catalyzes hydrolysis of maltose into glucose is named as maltase</li> </ul> <p>$C_ {12} H_ {22} O_ {11}$ $\xrightarrow{Maltase}$ $C_ 6 H_ {12} O_ 6$</p> <ul> <li>Sometimes enzymes are also named after the reaction where they are used</li> <li><strong>Example -</strong> enzymes which catalyse the oxidation of one substrate with the simutaneously reduction of another substrate are named as oxido reductase enzymes</li> </ul> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-267-1954.8.jpg"></p> </div>

<div> <h3 id="successthank-yousuccess"><Success>Thank you</Success></h3> </div> <div style='float: right; width:0%;'> <p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-10-biomolecules-l-10_12-qli5oe-k8pe-312-2352.0.jpg"></p> </div>