At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be:
a. 98% Vmax (show your work) (2)
b. 99% Vmax (answer only) (1)
c. 99.9% Vmax (answer only) (1)
The rate of an enzymatic reaction can be calculate using the Michaelis-Menten model, which states that the rate is given by:
When the rate is 98% Vmax, we have:
Which can be rearranged to calculate the concentration of substrate as a function of KM.
With an analogous calculation, for rate = 99% of Vmax we arrive to:
And for rate = 99.9% of Vmax:
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does...
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
What is the rate of an enzyme catalyzed reaction if the Vmax is 100µmol S→P/min and the Km is 7 mM and the substrate concentration is 11mM? Is the enzyme working at Vmax? What if the substrate concentration is raised to 25mM?
Vmax of an enzyme-catalyzed reaction is A. the rate observed when the enzyme active sites are saturated with substrate B. independent of the amount of enzyme present C. the rate observed at the highest substrate concentration that can be experimentally obtained D. the initial rate observed at very low substrate concentrations
biochemistryAn uncompetitive inhibitor of an enzyme catalyzed reaction a. binds to the ES complex b. is without effect at saturating substrate concentration. c. can actually increase reaction velocity in rare cases. d. decreases Vmax e. Binds to Es completx and lowers Vmax
Under what circumstances does an enzyme catalyzed reaction rate resemble a non-enzyme catalyzed reaction? At very low concentrations of substrate (Km is greater than S) the Michaelis-Menton equation can be simplified to? At very high concentrations of substrate, the Michaelis-Menton equation can be simplified to? How do you determine the initial rate of reaction
5. The Km of an enzyme of an enzyme-catalyzed reaction is 6.5 uM. What substrate concentration will be required to obtain 55% of Vmax for this enzyme? (10 pts)
The initial rate, V, of an enzyme catalyzed reaction varies with substrate concentration as follows: 106 x Initial rate, Ms SJ, M 0.020 0.585 0.004 0.495 0.002 0.392 0.001 0.312 0.250 0.00066 Determine Vmax and Km for this reaction
Consider the enzyme-catalyzed reaction with Vmax=164 (μmol/L)min−1 and KM=32μmol/L. Part A If the total enzyme concentration was 6 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? Express your answer to three significant figures. kcat kcat = 2.73×104 min−1 Part B Calculate kcat/KM for the enzyme reaction.
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...