1. R max and K m (26.4) Constants from Michaelis-Menten equation give insight into qualitative and quantitative aspects of enzyme kinetics Constants – Indicate if enzyme inhibition is present and what type of inhibition is exhibited – R max is the maximum possible rate of conversion of substrate to product for a given enzyme – K m is related to how tightly an enzyme binds a substrate (the higher the value, the less tightly bound the substrate) Inverting the Michaelis-Menten rate law gives an equation that can be useful for obtaining the maximum rate and the Michaelis constant – Lineweaver-Burk plot is generated by plotting 1/rate vs. 1/[S] Lineweaver-Burk plot Lineweaver-Burk equation is more useful for getting constants since experiments can be done over a short range of substrate concentrations – y-intercept gives us R max, which is then used with the slope to get K m

2. Enzyme Inhibition (26.4) Inhibition is a term used to describe the inability of a product being formed due to the presence of another substance (the inhibitor) – Enzyme inhibition can be competitive or noncompetitive Enzyme inhibition Competitive inhibition is caused when an inhibitor “competes” with the substrate in binding with the enzyme – Inhibitor decreases production of ES, thus decreasing product formation Noncompetitive inhibition is caused when an inhibitor can bind to either the free enzyme or the enzyme-substrate complex – Inhibitor does not allow ES complex to convert to products

3. Michaelis-Menten Plot for Catalyzed Reaction of CO 2 with H 2 O

4. Lineweaver-Burk Plot for Catalyzed Reaction of CO 2 with H 2 O

5. Enzyme Inhibition