Chapter-10 Enzymes FB (4)

Chapter-10 Enzymes FB (4) - Chapter 10 Enzymes...

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Chapter 10: Enzymes Classification, Kinetics and Control
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Reference of material in Devlin’s text Classification of enzymes 378-382 Coenzymes and Cofactors 390-395 Concept of enzyme mechanism 382-386 Enzyme kinetics 397-404 Enzyme inhibition 407-409 Enzyme regulation 413-114
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History and two major properties of enzymes Earlier known as ferments First enzyme isolated was Urease by James Sumner 1926 Enzymes speed up the rate of reaction Enzymes are very specific in their action
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Classification of Enzymes
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Oxidoreductases, Transferases and Hydrolases
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Lyases, Isomerases and Ligases
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Enzyme + Cofactors Inorganic Metal ions Needed for optimal activity of the enzymes
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Examples of Cofactors
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Coenzymes Enzyme + Organic molecules Needed for optimal activity of the enzymes
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Examples of Coenzymes
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Prosthetic group Enzyme Organic molecules Inorganic Metal ions
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Prosthetic group Cofactor Inorganic complexes Coenzyme Organic complexes Dissociable Cofactor/Coenzyme Tightly bound and stay with enzyme Prosthetic group or
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Apo- and holo-protein/enzyme
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How Enzymes Work? Enzyme Active site
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Lock and Key Hypothesis
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Induced Fit Hypothesis
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How enzymes speed up the rate of reaction? Review the concept of Gibbs free energy change- G
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Predicting whether or not a process is spontaneous. Spontaneous processes have a negative free energy change, ΔG is negative or less than zero . The system releases energy to its surroundings as the process occurs. This kind of change is an exergonic process, ΔG = - . The size of the free energy change indicates the "driving force" behind the reaction. The bigger and more negative the DG the more likely the process. A reaction with a DG = -623,400 kcal has a better chance of happening than a reaction with a DG = -500 kcal. The reactants change into products, release the stored energy and gradually the system reaches a stable condition of equlibrium.
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