Enzymes & Chemical Reactions<br />
What is Energy???<br />
LAWS<br />First Law of Thermodynamics –<br />	Energy is not created nor destroyed, just changed from one form to another<b...
Free Energy <br />∆G  - Change in free energy<br />Exergonic – Release of free energy.  Spontaneous reactions and ∆G is le...
Enzymes & Catalysis<br />
Transition state<br />Activation energy<br />Reactants<br />Products<br />
Transition state<br />Ea with enzyme<br />Reactants<br />∆G does not change<br />Products<br />
Induced Fit<br />Enzyme<br />Substrate<br />
Figure 3-22<br />A MODEL OF ENZYME ACTION<br />Transition state<br />Products<br />Substrates<br />Enzyme<br />Shape chang...
Competitive Inhibition<br />Enzyme<br />Substrate<br />
Allosteric Regulation<br />Enzyme<br />Substrate<br />
Figure 3-25a<br />Enzymes from different organisms may function best<br />at different temperatures.<br />Glucose-6-phosph...
Figure 3-25b<br />Enzymes from different organisms may function best<br />at different pHs.<br />Chitinase from soil-dwell...
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Enzymes & chemical rxns

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  • Kinetic, PotentialThermal energy – kinetic energy of molecular motion.What is the difference b/t heat and temperature?
  • Cofactors- Ions such as Zinc (Zn) or magnesium (Mg) or small organic molecules called coenzymes.
  • Enzymes & chemical rxns

    1. 1. Enzymes & Chemical Reactions<br />
    2. 2. What is Energy???<br />
    3. 3. LAWS<br />First Law of Thermodynamics –<br /> Energy is not created nor destroyed, just changed from one form to another<br />Second Law of Thermodynamics- <br /> Entropy always increases in a closed system. ie. Physical & chemical processes proceed in the direction that results in lower potential energy & increased disorder. <br />
    4. 4. Free Energy <br />∆G - Change in free energy<br />Exergonic – Release of free energy. Spontaneous reactions and ∆G is less than zero.<br />Endergonic – Require input on energy. Non spontaneous and ∆G is greater than zero.<br />
    5. 5. Enzymes & Catalysis<br />
    6. 6. Transition state<br />Activation energy<br />Reactants<br />Products<br />
    7. 7. Transition state<br />Ea with enzyme<br />Reactants<br />∆G does not change<br />Products<br />
    8. 8. Induced Fit<br />Enzyme<br />Substrate<br />
    9. 9. Figure 3-22<br />A MODEL OF ENZYME ACTION<br />Transition state<br />Products<br />Substrates<br />Enzyme<br />Shape changes<br />1.Initiation: Reactants bind to the active site in a specific orientation, forming an enzyme-substrate complex.<br />2.Transition state facilitation: Interactions between enzyme and substrate lower the activation energy required.<br />3.Termination: Products have lower affinity for active site and are released. Enzyme is unchanged after the reaction.<br />
    10. 10. Competitive Inhibition<br />Enzyme<br />Substrate<br />
    11. 11. Allosteric Regulation<br />Enzyme<br />Substrate<br />
    12. 12. Figure 3-25a<br />Enzymes from different organisms may function best<br />at different temperatures.<br />Glucose-6-phosphatase from bacterium that lives in hot springs<br />Glucose-6-phosphatase from bacterium that lives inside humans<br />
    13. 13. Figure 3-25b<br />Enzymes from different organisms may function best<br />at different pHs.<br />Chitinase from soil-dwelling bacterium<br />Chitinase from bacterium that lives in acidic pools<br />

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