Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 18, Problem 21P
Interpretation Introduction

Interpretation:

The correct option regarding the phosphofructokinase should be identified.

Introduction:

Phosphofructokinases are kinase group of enzyme, phosphorylates fructose-6 phosphate by utilizing ATPs.

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You are studying the kinetics of a novel competitive inhibitor of ATP-citrate lyase that can be used to prevent obesity. What is likely true about this inhibitor? (A) This inhibitor lowers the Vmax of ATP-citrate lyase. (B) The inhibitor likely looks structurally similar to acetyl CoA. (C) The inhibitor binds to an allosteric region on ATP-citrate lyase and prevents catalysis. (D) You can distinguish between an uninhibited and inhibited enzyme by comparing the x-intercepts on a Lineweaver-Burk plot. (E) This inhibitor lowers the KM of ATP-citrate lyase. Related to this question, you should also be able to: • explain the function of ATP-citrate lyase and why inhibition would prevent obesity • interpret Michaelis-Menten & Lineweaver-Burk plots related to this question • explain the differences between a competitive and non-competitive inhibitor
The following are the negative regulators of phosphofructokinase except Select one:  a. AMP +b. H  c. Citrate  d. ATP
The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme.     (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP?   (b) In what ways is glycolysis regulated by ATP levels?   (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained?   *A graph is included for this question*
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