Select all that applies How does ATP regulate the activity of PFK-1?ATP binds to PFK-1 at the catalytic site as a competitive inhibitor, decreasing PFK-1 activity.ATP binds to the catalytic site as a substrate, increasing PFK-1 activity.ATP binds to the allosteric site as an activator, increasing PFK-1 activity.ATP binds to the allosteric site as an inhibitor, decreasing PFK-1 activity.

ATP plays a crucial role in regulating the activity of phosphofructokinase-1 (PFK-1), an enzyme…

Answered: How does ATP regulate the activity of…

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 statements regarding the active site of cytochrome P450s is correct? Cytochrome P450-catalyzed monooxygenation proceeds with low stereoselectivity Cytochrome P450-catalyzed monooxygenation requires two electrons supplied by the redox process involving NADPH and NADP+. The 5th distal position (below the plane of the porphyrin ring) in cytochrome P450 is always occupied by His Cytochrome P450 is responsible for the metabolism of the minority of prescription drugs Cytochrome P450 contains manganese
which answer is false
PFK-1 is actually a tetramer with four identical active sites that produced fructose 1,6-bisphosphate. There are also allosteric sites for citrate and ATP/ADP on each subunit as well which influence how well the active sites are binding substrates or producing product. The arginine at position 48 on each PFK-1 subunit normally forms a salt bridge with a negatively charged oxygen on phosphate in the catalytic interface of PFK-1. Speculate on how the R48C mutation might change this function.
please see attached
Sketch the arrow pushing mechanism of the hydrolysis of phospho-serine by the emzyme phosphatase. The enzyme has a catalytic diad. Cys (pka 8.2) and glu (pka 4.3)
How is cigarette smoking related to elastase function? Methionine sulfoxide is formed by cigarette smoke in the antitrypsin protein, which leads to the full manifestation of the disease in individuals heterozygous for emphysema. Oxidation of methionine 358 by cigarette smoke of the elastase inhibitor active site leads to an increased inhibition of elastase and subsequent overaccumulation of mucus in the lungs. The inhibitor of elastase is axidized by cigarette smoke so elastase doesn't function properly in healthy individuals. Cigarette smoke modifies the elastase methionine residues such that the enzyme activity is blocked.
Refer to Figure 3 which shows the relationship between phosphofuctokinase-1 (PFK-1) activity and fructose 2,6-bisphosphate. 100 +F2,6BP 80 60 40 -F2,6BP 20 0.05 0.1 0.2 0.4 0.7 1.0 2.0 4.0 EFructose 6-phosphate] (mm) Figure 3 (i) Explain the PFK-1 activity in the absence and presence of fructose 2, 6- bisphosphate. (ii) Explain the effect of increased ATP on PFK-I PFK-1 activity (% of Vma)
Which enzyme catalyzes the reaction?
What compound(s) were the most effective inhibitors and what compound(s) were the most effective activators?
What advantage is there to phosphoglycerate kinase having an open and closed protein configuration? It allows water to be trapped in the active site along with the substrate. O Changing of the configuration of the enzyme makes the reaction exergonic. The induced-fit mechanism maximizes accessibility of active site without sacrificing hydrophobic environment. It forces covalent binding of the substrate to the enzyme active site.
Why is it important that the hexokinase reaction have a large negative deltaG? Would the cell be able to generate/store energy if the deltaG were close to zero? The GAPDH reaction uses an active site cysteine to catalyze the reaction. How would replacing the cysteine by serine affect the reaction? Why do kinases require magnesium to function well?
In a cell with abundant energy (in the form of ATP and NADH), and also glucose and other carbohydrates to break down, it might be advantageous to store some of that glucose in the form of glycogen. Which of the enzyme(s) (hexokinase, G6P isomerase or PFK-1) do you think is most likely to be inhibited in order to divert those carbohydrates into the synthesis of glycogen for storage? Why?

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