Consider the reaction coordinate diagram shown below. Which of the following are true?(Pick two.)-Free energySubstrateReaction progressProductAG°' < 0AG°' = 0AG°' > 0AG of the forward reaction > AG of the reverse reaction.AG of the forward reaction < AG of the reverse reaction.

We know energy change in a reaction can be calculated as difference between energy of product to the…

Answered: Consider the reaction coordinate…

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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Which of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.
Consider the two reactions below. They are fast and have reached equilibrium by the end of the time shown. At time zero (t = 0) which is true? [Product] (M) I 2 1 Time The AG of reaction 1 is greater (more positive) than the AG of reaction 2. The AG of reaction 1 is less (more negative) than the AG of reaction 2. ○ The AG of reaction 1 is equal to the AG of reaction 2.
Most of the enzyme reactions followed the mathematical kinetic plots suggested by the Michaelis-Menten plots:viii. Draw another Lineweaver-Burk plot and on the same plot, draw a graphto indicate un-competitive inhibition.Note: In the graphs, lable Vmax and KM clearly.
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
The 2 eynzymes are affected by a substrate. Choose all correct answers.
assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators
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The enzyme enolase has a permanently bound Mg2+ ion in its active site. To the below is a schematic of the enzyme active site bound to an intermediate of the reaction. Which of the following are true? (Pick two.) PO32- Н Mg2 C C H HO Favorable electrostatic interactions (dashed blue lines) between Mg2+ and the intermediate increase (make it more positive) the AG of the reaction. Favorable electrostatic interactions (dashed blue lines) between Mg2+ and the intermediate decrease (make it more negative) the AG of the reaction. Favorable electrostatic interactions between Mg2+ and the intermediate decrease the rate constant, k, of the reaction, decreasing the rate of the reaction. Favorable electrostatic interactions between Mg2+ and the intermediate increase the rate constant, k, of the reaction, increasing the rate of the reaction.
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.

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Consider the reaction coordinate diagram shown below. Which of the following are true? (Pick two.) - Free energy Substrate Reaction progress Product AG°' < 0 AG°' = 0 AG°' > 0 AG of the forward reaction > AG of the reverse reaction. AG of the forward reaction < AG of the reverse reaction.