Lectures 19, 20, 21 Oct 3-5 - Enymes and Kinetics

Lectures 19, 20, 21 Oct 3-5 - Enymes and Kinetics - Enzyme...

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Enzyme Specificity through the enzyme active site Enzymes are the most specific catalysts known, and their specificity is the result of the distinct substrate binding site within the enzyme. The enzymes tertiary structure creates a precise pocket for an individual substrate, using amino acid residues to provide the necessary charge and hydrophobic characteristics to accommodate any type of molecule as substrate. Two models accounting for an enzyme’s specificity were proposed:
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Asymmetry of the binding site. Enzymes cannot only differentiate isomeric compounds, but also distinguish between two equivalent atoms in symmetrical or prochiral molecules if the center is asymmetric. (eg. Glycerol). The enzyme only binds one orientation of the symmetrical molecule. This requires specific recognition of three specific binding sites on the enzyme for the single molecule (see below):
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Mechanisms of catalysis: All chemical reactions, catalyzed or not, have a potential energy barrier associated with the reaction. The reaction cannot proceed until
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Lectures 19, 20, 21 Oct 3-5 - Enymes and Kinetics - Enzyme...

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