BCHM 310 Lecture Notes - Lecture 29: The Intercept, Uncompetitive Inhibitor, Enzyme Kinetics

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Knowledge (or measurement) of km and v max for one enzyme with a variety of substrate can provide infor for what is important for substrate binding, the reaction and how the enzyme is catalyzing the reaction. So, how e binds s + catalyzes the reaction. For example, if we compare s1 and s2 with one enzyme --> two arbitrary substrates. If the km for s1 is less than the km for s2. And vmax for s1 is equal to k max for s2. Vmax = kcat * the amount of enzyme present. Thus, we can conclude that s1 binds more tightly than s2. Also, conclude no change in double dagger (transition state) stability. You may find a slight diff in km or major diff in v max tells you one of the reactants has a harder time getting to the transition state.

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