6The AG of a reaction is positive. Which is TRUE?The cell cannot catalyze this reaction under any conditions.OThis reaction can only go forward in the cell if ATP is used.AG-AG in the cell, regardless of substrate/product concentrations.This reaction can go forward in the cell if the overall pathway has a negative AG.This reaction can go forward in the cell if the overall pathway has a positive AG.00

In a general reaction such as: A + B ⇌ C + D At equilibrium (steady state), the concentration of…

Answered: The AG of a reaction is positive. Which…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-
An enzyme-catalyzed reaction has a Km of 4 mM and a Vmax of 5x10-3 uM/s. What is the reaction velocity when the substrate concentration is: 5 mM 4 mM
An enzyme catalyzes the reaction A --> B. The enzyme is present at a concentration of 2 nM, and the Vmax is 10 uM/s. The Km for substrate A is 10mM At what substrate concentration would this enzymatic reaction be operating at only 20 percent of its maximum rate?
Draw each of the enzymatic step for each chemical conversion and write the enzyme together with the co-factor for the steps where a co-factor is involved. How many carbons are transferred in the conversion from step 1 into the intermediate from step 2? Step 1 OH ACP-s ? (multiple enzymatic steps) OH OH Step 2 ACP-S R1 5..
The enzyme – catalyzed conversion of a substrate at 25°C has Michaelis constant of 0.04 mol L-!. The rate of the reaction is 2.45x104mol Ls1when the substrate concentration is 0.890 mol L. What is the Enzyme concentration and what is the maximum velocity? إجابتك
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site
How can an unfavorable reaction (AG°¹ > 0) still occur in a metabolic pathway? By increasing the temperature under physiological conditions. This reaction cannot be used in metabolic pathway reactions. It is linked to a favorable reaction. It is linked to another unfavorable reaction.
Which of the following equations accurately shows enzyme-catalyzed conversion of substrate to product? O E+S- ESP E+P O E+S- EP E + P OE+S+ ES E + P O E+S- ES E+P
Which of the following statements is true for the shown reaction? Substrate level phosphorylation occurs during the reaction Phosphoryl transfer occurs during the reaction Both A and B Neither A nor B
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C
When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. Afte reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors

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