Consider the reaction catalyzed by PFK. In the presence of ATP, which of thefollowing will be expected? Select all that apply.The T-state is stabilizedThe rate of the reaction is enhanced.The initial velocity plot would show a shift in the curve to the rightThe quaternary structure of PFK is stabilized to promote efficient binding of substrate

Phosphofructokinase-1 (PFK-1) is a glycolytic enzyme that catalyzes the transfer of a phosphoryl…

Answered: Consider the reaction catalyzed by PFK.…

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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Give all the reactions that will produce ATP either by substrate-level phosphorylation (SLP) or by oxidative phosphorylation (OP). If the given require a shuttle system, please indicate both MA shuttle and GP shuttle and give the ATP produced. Given: fructose 6-phosphate to 2pyruvate
V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V- Binding Change Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O The open conformation releases ATP. Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose. O Binding of ADP + P¡ drives change from open to loose. Hydrolysis of ATP to ADP + Pj drives the change from open to loose.
Can you explain the answe?
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?
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If the allosteric coefficient for ATCase increases from 250 to 1300, the rate of the N-carbamoylaspartate formation: O stays the same and the sigmoidal curve of reaction rate as a function of substrate shifts up. O decreases and the sigmoidal curve of reaction rate as a function of substrate shifts to the left. O increases and the sigmoidal curve of reaction rate as a function of substrate shifts to the left. O stays the same and the sigmoidal curve of reaction rate as a function of substrate shifts to the right. O decreases and the sigmoidal curve of reaction rate as a function of substrate shifts to the right. Question 9 Which of the following CANNOT be targeted for phosphorylation to modulate the activity of an enzyme? O Ser Ala O None of the amino acids listed can be targeted for phosphorylation to modulate enzyme activity The Tyr
Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.
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.
GAP + Pi + NAD+ ⟹1,3-BPG + NADH (Reaction 1) 1,3-BPG + ADP ⟹ 3-PG + ATP (Reaction 2) Which of the following statements concerning the information above is true? Select all that apply. A.Reaction 2 is an example of substrate level phosphorylation B.These reactions are written in a direction that would indicate gluconeogenesis is occurring in the liver C.The linking of Reaction 1 and Reaction 2 by the intermediate 1,3-BPG is an example of coupling of reactions D.Reaction 1 shows a redox reaction where the carbon skeleton is oxidized to generate electrons for a soluble electron carrier E.These reactions are irreversible under cellular conditions
The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?
When ATP and xylose are added to hexokinase, the enzyme produces a small amount of xylose-5-phosphate along with a large amount of ADP. How does this observation support the induced fit model?
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