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Lecture 12

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Wilfrid Laurier University
Matthew Smith

 Clicker question answers: o Most of the potential energy stored in ATP that is available to drive cellular reactions is found in the bonds b/w phosphate groups  Enzyme Specificity o Typically one active site; may be many binding sites o Enzyme is a little more open when there is no substrate; when there is a substrate attached at the binding site, the enzyme changes a bit in shape by enclosing the substrate in the enzyme  Catalytic Cycle of Enzymes o Key and lock (only specific keys (substrates) can fit into certain locks (enzymes))  Induced Fit Hypothesis --> variation of lock and key hypothesis  Enzyme changes its shape in order to better fit the substrate   Recognizes molecule of lactose (disaccharide); this enzyme cuts that lactose in half to produce galactose and glucose which can be used for energy or other purposes  The cleaving of the molecules causes a slight change in structure of the enzyme which allows the release of the two products  Enzyme Cofactors o Inorganic ions/organic nonprotein groups necessary for the occurrence of catalysis o Cofactors  Metallic ions (Mg , Fe , Cu , Zn )+  Aren't needed in high amounts o Coenzymes  Organic cofactors (i.e. vitamins)  Usually larger cofactors  Usually specific to certain enzyme activities  Absolutely required for catalysis  Transition State o During catalysis, the substrate and active site form an intermediate transition state  Reduce activation energy to transition state o Enzymes facilitate the formation of transition state via 3 major mechanisms: Bringing reacting molecules into close proximity Exposing reactant molecule to altered environments that promote their interactions Changing shape of substrate m
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