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
Under what circumstances does an enzyme catalyzed reaction rate resemble a non-enzyme catalyzed reaction? At very...
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
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K? Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
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)
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)
2-In an enzyme-catalyzed reaction, the rate of the reaction depends on which of the following at very low substrate concentrations? Select one: Neither enzyme concentration nor substrate concentration Enzyme concentration but not substrate concentration Substrate concentration but not enzyme concentration Both substrate concentration and enzyme concentration
Use the Michaelis-Menton equation, what is the velocity of an uninhibited enzyme (catalyzed reaction)? What is the enzyme’s turnover number given the following data: Km=4x10 ^-8M ; [S]=½ Km ; Vmax= 6.0 nmole/L•sec ; Et=1.0x10 ^ -10M.)
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
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...
The concentration of substrate X is low. What happens to the rate of the enzyme- catalyzed reaction if the concentration of X is doubled? 15. What effect does an increase in the enzyme concentration have on the rate of an enzyme-catalyzed reaction? 16.
3) Enzyme kinetics are determined under initial rate conditions, wherein the initial substrate concentrations changes very little, because: (A) Products do not accumulate and inhibit the forward reaction (B) Enzymes are unstable under most assay conditions, and rapidly lose activity (C) The substrate concentration does not change appreciably and so does not create an additional variable (D) All of the above (E) Some of the above