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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Free energy (G) W+X Figure 6.2 Select one: O a. A O b. Y+Z O c. c O d. B O e. с W+X K Direction of reaction B Answer the question using the accompanying graph. Which portion of the graph shows the activation energy in the absence of enzyme? Y+Z
Which of the following is incorrect? a. The ratio "catalyzed rate/uncatalyzed rate" is known as catalytic power b. Most enzymes exhibit a higher degree of specificity than non-biologic catalysts O c. Most enzymes are proteins; but a few are RNA molecules Od. Most enzymes exhibit a higher catalytic power than non-biologic catalysts
Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
In lab 4, you calculated cholesterol levels of a sample directly based on the absorbance ratio of the sample to standard. What assumption are we making for this calculation to be accurate? O All the cholesterol in the sample is unesterified (i.e. free cholesterol). There is a linear relationship between the cholesterol concentration of the sample and the absorbance of the sample. The enzymatic reaction goes to completion, i.e. all substrates are converted to products. The HDL and LDL in the sample have different absorption maxima as compared to the cholesterol.
the Km of an enzyme for its substrate is 50mM. At what concentration of substrate would the enzymaticslly catalyzed reaction be at 60% maximum - 30 - 60 -75 - 50 -80
Sketch a graph showing how the concentration of product P varies with time for chymotrypsin-catalysed hydrolysis using a substrate that displays both Michaelis-Menten kinetics and burst kinetics. On the same graph show the effect of doubling the enzyme concentration, keeping all other conditions the same.
An enzyme A is most active at 37oC. Which of the following change will increase the activity of A? Question 9 options: Increasing the enzyme temperature from 20 oC to 37 oC. Decreasing the enzyme temperature from 37 oC to 25 oC. Increasing the enzyme temperature from 37 oC to 47 oC.
Bypass reaction in the anabolic pathway often occurs when A The ΔG of the reverse reaction in the catabolic pathway has a large negative value B The ΔG of the reverse reaction in the catabolic pathway has a large positive value C The ΔG of the reaction in the anabolic pathway is close to zero D The ΔG of the reaction in the anabolic pathway is positive E None of the above
Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
When substrate concentration [S] << Km, the rate of an enzymatic reaction is increased by O increasing kcat/Km O increasing total enzyme concentration O increasing [S] O A and B O A, B and C
Here’s a kinetic model for some enzyme E acting on substrate S. Give the equation for the change in the concentration of free enzyme (E) with time.
This reaction an enzymatic and reaction has kinetic constants k1, k-1, and k2 were found to be 107 M/s, 4.1-104/s1, and 10²-s1, E+ P What is Km? E+S ES

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