Which one of the following is true regarding our coverage of enzyme kinetics? Increasing the concentration of an enzyme is not expected to affect the Km of the enzyme. One strategy for increasing Vo if the enzyme is not already saturated is to reduce enzyme concentration. For a favorable reaction, the G value of a transition state has a value that is lower than the G value of the reactant but higher than the G value of the product. An enzyme that is a high-Km mutant has a slower turnover rate than the wild-type enzyme. Enzymes that obey Michaelis-Menten kinetics have approximately zero-order kinetics when [S] is 10% of Km or lower.

Which one of the following is true regarding our coverage of enzyme kinetics? Increasing the concentration of an enzyme is not expected to affect the Km of the enzyme. One strategy for increasing Vo if the enzyme is not already saturated is to reduce enzyme concentration. For a favorable reaction, the G value of a transition state has a value that is lower than the G value of the reactant but higher than the G value of the product. An enzyme that is a high-Km mutant has a slower turnover rate than the wild-type enzyme. Enzymes that obey Michaelis-Menten kinetics have approximately zero-order kinetics when [S] is 10% of Km or lower.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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The enzyme examase catalyses the following reaction, A - B where A is the reactant and B is the product A595 measurements were used to determine the catalytic activity of examase by measuring the rate at which B is produced. From this, the activity of the enzyme was determined to be 42 µmol/mL per minute. A standard albumin solution (concentration = 10 mg/mL) was used to prepare a standard curve of Abs595 vs amount of protein in mg. The protein assay was also performed using 100 uL of a 1 in 10 dilution of the original examase sample. For the absorbance measurements, it was determined that the sample used in the A595 measurement contains 1.2 mg of examase. Which of the following statements correctly gives the specific activity of examase? 1.0.35 U/mg O 2.0.035 U/mg 3. 5040 U/mg O 4.35 U/mg O 5.3.5 U/mg
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Question 33
what is the approximation used to derive the reaction rate for an enzyme catalysed reaction that proceeds by a michaelis menten mechansim
Use the reaction energy diagram above to answer the following questions.
In order to describe the reaction sequence of two different substrates catalyzed by an enzyme; E + S1 ↔ ES1ES1 + S2 ↔ ES1S2ES1S2 → P + E a.Derive the rate equation for the reaction with the Michaelis-Menten assumption. b.Simplify the derived rate equation for reaction conditions where the S1 substrate concentration is much higher than the S2 substrate concentration.
If the substrate concentration is twice the KM of an enzyme. The initial velocity (Va) is going to be of the maximum velocity (Vmax) according to Michaelis-Menten (MM) equation, Hint: Use the MM equation to arrive at the answer. O 1/2 O 1/4 O 1/3 O 2/3
Why do most living organisms have an enzyme to decompose hydrogen peroxide? Ideal Gas and Decomposition of Hydrogen Peroxide Quiz Because hydrogen peroxide is present in many foods. Because hydrogen peroxide is toxic and needs to be destroyed. Because hydrogen peroxide does not dissolve in water. Because hydrogen peroxide is produced in the liver.
14.
Protein phosphatase 1 (PP1) helps regulate cell division and is a possible drug target to treat certain types of cancer. The enzyme catalyzes the hydrolysis of a phosphate group from myelin basic protein (MBP). The activity of PP1 was measured in the presence and absence of the inhibitor phosphatidic acid (PA). [MBP] (mg-mL-¹) 0.010 0.015 0.025 0.050 Vo without PA (nmol-mL-¹ min-¹) 0.0209 0.0355 0.0419 0.0838 Use the data in the table to construct a Lineweaver-Burk plot. What type of inhibitor is phosphatidic acid? Uncompetitive Noncompetitive Mixed inhibition Competitive Vo with PA (nmol-mL-¹ min-¹) 0.00381 0.00620 0.00931 0.01400
Carbonic anhydrase is one of the fastest enzymes known. If 10 µg of this enzyme catalyzes the conversion of 0.30 g of CO2 to bicarbonate in 1 minute at 37˚C. What is the Kcat value for this enzyme in min -1?
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