Lectures 7-10 - k cat[ES[E[S[ES =(k-1 k cat/k 1[E T-ES[S[ES...

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Enzymes Enzymes are biological catalysts that speed up chemical reactions by several orders of magnitude Enzymes are highly specific in terms of reactions Enzymes affect reaction rates, not reaction equilibria
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Enzyme Kinetics
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Enzyme Kinetics Enzyme lowers activation energy barrier for chemical reactions
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Enzyme Kinetics Binding of substrate to enzyme happens at the active site Lock and Key Model Induced Fit Model
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Enzyme Kinetics Effect of enzymes on reaction rates can be calculated by changing initial concentration of substrate with time
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D[ES]/dt = 0; [E T ] = [E] + [ES] Forward rate = Reverse rate k 1 [E][S] = k -1 [ES] + k cat [ES] k 1 [E][S[ = (k -1
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Unformatted text preview: +k cat )[ES] [E][S]/[ES] = (k-1 +k cat )/k 1 ([E T-ES])[S]/[ES] = K m ([S][E T ] - [S][ES])/[ES] = K m [E T ][S]/[ES] - [ES][S]/[ES] = K m [E T ][S]/[ES] - [S] = K m [E T ][S][ES] = K m +[S] [E T ][S] = (K m + [S])[ES] [ES] = [E T ][S]/(K m + [S]) …recall v o =k cat *[ES] v o /k cat = [E T ][S]/(K m + [S]) v o = k cat [E T ][S]/(K m + [S]) …recall V max = k cat *[E T ] v o = V max [S]/(K m + [S]) Derivation of Michaelis-Menten Equation Enzyme Kinetics Lineweaver-Burk plot Michaelis-Menten curve Enzyme Kinetics Enzyme Inhibition Enzyme Inhibition Enzyme Inhibition Enzyme Inhibition Enzyme Inhibition...
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Lectures 7-10 - k cat[ES[E[S[ES =(k-1 k cat/k 1[E T-ES[S[ES...

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