Consider the reaction catalyzed by PFK. In the presence of ATP, which of the following will be expected? Select all that apply. The T-state is stabilized The rate of the reaction is enhanced. The initial velocity plot would show a shift in the curve to the right The quaternary structure of PFK is stabilized to promote efficient binding of substrate
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- A hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration 50mM at 50% of Vmax. Find the substrate concentration when the velocity of reaction is equal to 75% of Vmax.Here’s a kinetic model for some enzyme E acting on substrate S. Give the equation for the change in the concentration of free enzyme (E) with time.Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor.
- In several species of bacteria, GAPDH activity is controlled by the NADH/NAD+ ratio. Does the activity of GAPDH increase or decrease when the NADH/NAD+ ratio increases? Explain. Assume that only the forward direction of the reaction is relevant. a) The activity of GAPDH increases when the NADH/NAD+ ratio increases. b) The activity of GAPDH decreases when the NADH/NAD+ ratio increases.Here’s a kinetic model for some enzyme E acting on substrate S. The last step (EP → E) is rate determining. Write an equation for the rate of the reaction. And write an equation for the total amount of enzyme in this system.Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.
- Consider the reaction catalyzed by PFK. In the presence of AMP, which of the following will be expected? Check all that apply: a)The Km for substrate would be decreased b) the initial velocity plot would show the curve shifted to the right c) the R state is stabilized d)the rate of the reaction is diminishedExplain the mechanism by whicha single substrate reaction catalyzed by an enzyme with a single binding sitefor the substrate is able to exhibit sigmoidal kinetics.With appropriate chemical reactions and with all the catalysts involved explain the differences between the MVA and MEP pathway.
- In a biochemical pathway, three ATP molecules are hydrolyzed. The endergonic reactions in the pathway require a total of 17.3 kcal/mole of energy to drive the reactions of the pathway. What is the overall change in free energy of the biochemical pathway? Is the overall pathway endergonic or exergonic?Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest substrate binding? Please explain. Part c) Which graph has the largest specificity or efficiency constant? Please explain.Give all the reactions that will produce ATP either by substrate-level phosphorylation (SLP) or by oxidative phosphorylation (OP). If the given require a shuttle system, please indicate both MA shuttle and GP shuttle and give the ATP produced. Given: fructose 6-phosphate to 2pyruvate