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 allosteric site as an 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. The graph shows the effect of ATP on the allosteric enzyme phosphofructokinase-1 (PFK-1).PFK-1 activity (% of Vmax)100806040200Low[ADP][ATP]High[ADP]For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but thereis a point beyond which increasing the concentration of ATP inhibits the enzyme.

The enzyme phosphofructokinase 1 (PFK-1) catalyzes the following reaction: Fructose 6-P + ATP –>…

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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Similar questions

Which of the following statements is TRUE regarding regulation of glycolyis? hexokinase regulates glycolysis by degrading glucose-6-phosphate low levels of ATP inhibit phosphofructokinase-1 because ATP preferentially binds to the allosteric inhibition site inhibition of glucose-6-phosphate by hexokinase is an example of feedback inhibition none of these statements are correct I selected option C and got it wrong, what is the correct answer with an explanation to why it is and also how was my answer wrong?
which answer is false
The three irriversible reactions in glycosis is : Hexoknase, PFK-1 and Pryvate kinases. they are all enzymes, why these three enzymes are irriversible? the explaination below is not very understandble. "Hexokinase: This enzyme catalyzes the conversion of glucose to glucose-6-phosphate. This reaction consumes ATP and traps glucose inside the cell by converting it into a charged and phosphorylated form. Phosphofructokinase-1 (PFK-1): This enzyme catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. This reaction is the committed step of glycolysis, and it is also the main regulatory point of the pathway. PFK-1 is allosterically inhibited by ATP and citrate and activated by AMP and fructose-2,6-bisphosphate. Pyruvate kinase: This enzyme catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate, producing ATP. This reaction is the last step of glycolysis and is also highly regulated. Pyruvate kinase is allosterically activated by fructose-1,6-bisphosphate…
The enzyme PFK was studied in mosquitos. The authors found that: PFK Vmax was 4.5 μmol/min with F-1,6-BP (along with ATP) as the substrates PFK KM using F-1,6-BP and ATP was 1.48 mM F-2,6-BP was a powerful activator for PFK PFK was inhibited by ATP PFK inhibition by ATP could not be overridden by AMP On the graph below, draw: a. A Michaelis-Menten curve for the normal mosquito PFK enzyme b. A Michaelis-Menten curve for the PFK enzyme activated by F-2,6-GP C. A Michaelis-Menten curve for the PFK enzyme inhibited by ATP d. A Michaelis-Menten curve for the PFK enzyme when ATP and AMP are both present
Match the descriptions and compounds with the terms competitive, uncompetitive, and noncompetitive inhibition. Competitive inhibition Uncompetitive inhibition Noncompetitive inhibition
What effect is seen on a Lineweaver-Burke graph when a competitive inhibitor is added to an enzymatic reaction? neither the y-intercept nor the slope change both the y-intercept and the slope change the slope of the line changes the line is inversed the y-intercepts changes
Consider the function of the cofactor FAD. Which of the following makes it unique (different) from NAD+? Select all that apply. O Operates as part of an enzyme and is not a mobile electron carrier O In its fully reduced state, carries 2 electrons OInvolved in electron transfers as part of pyruvate dehydrogenase complex activity O Facilitates single electron transfers
Box lists options: Thioredoxin is: oxidized, reduced activity causes the: inhibition, activation enzymes by: forming, eliminating there is: reduced, oxidized Benson cycle is: more, less
State and describe the three different types of inhibitors which are competetive, uncompetetive and mixed inhitition. short answer please.
You experiementally apply the compund antimyctin, which inhinits the functioning of complex III, cytochrome reductase, from participating in redox reactions. You follow this with the addition of 6 molecules of FADH2. How many total ATP molecules can be created using the number of protons that were pumped?
A newly discovered enzyme from the South African marine sponge symbionts was shown to catalyze the oxidation of two substrates (A and B) at different rates. The KM for substrate A was 200 mM and the KM for substrate B was 25 mM. Which is the most likely natural substrate for this enzyme?
During the substrate-level phosphorylation reaction of the TCA cycle, _______________ is phosphorylated to _________________. The energy for this phosphorylation comes from breaking down the _______________________________ bond of _______________________________, releasing a ____________________________ Use the words below CTP CDP GDP Sulfhydryl CoASH Succinyl CoA Acetyl CoA Phosphoanydride α-ketoglutarate GTP Phosphodiester Thioester

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