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...

See similar textbooks

Similar questions

6. Draw in arrows to indicate electron flow (mechanism) for the below step in the catabolism of glucose (glycolysis). (Hint: there are 16 arrows in this mechanism). Base Enzyme H H- HC C=0 H-A -OH CH₂OPO 20 Enzyme 203PO- H S H-A H -OH CH₂OPO₂2€ Base Base Enzyme H- -H OH CH₂OPO₂2 Enzyme SH CONH₂ + NAD e 203PO, H- + NADH/H -OH CH₂OPO₂² Enzyme H+O H-A -OH CH₂OPO₂²8
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
A true transition state can bind to an enzyme active site with a KT as low as 7.00×10-26 M. This is a remarkable number, with interesting consequences. Consider a hypothetical solution of an enzyme in equilibrium with a ligand that binds with a Kp of 3.45×10-27 M. a If the concentration of free enzyme, [E], is equal to the concentration of the enzyme-ligand complex, [EL], what would [L], the concentration of free ligand, be? [L] = M
5 of 5 7. When a catalyst is added to a reaction the activation Energy is (increased or decreased), (more or less) energy is needed to react the new activated complex, and (more or less) collisions have sufficient energy to (increase or decrease) the reaction rate.
Using this graph, what can be determined about the effect of enzyme concentration on the initial rate of the reaction and on the amount of product formed?
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.
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.
How does Kcat influence the velocity of MM enzymes ? A. Linear relationship B. Inverse relationship C. No effect D. Only effects velocity if total enzyme concentration is low v = Vmax [S] KM + [S] Turnover rate kcat = Vmax [ET] Speed (substrates product/sec)
The peak on the blue line marked by the #2 represents which of the following? Free energy, G Transition state (‡) S 2 3 ES EP 4 AG* P uncat Reaction coordinate JAG cat The energy required for the enzymatic conversion of substrate to product. The binding energy (AGB) of the substrate binding the enzyme. Desolvation of the substrate and the active site of the enzyme.. Solvation of the product and the active site of the enzyme..
:The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics Vo (mmol/min) S (mmol/L) 0.8 3 4 217 325 433 488 1,000 :The Km for this enzyme is approximately 647 mM 4 O mM 1 O mM 1,000 Ⓒ mM 3 O mm 6 O