Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 19, Problem 8P
Interpretation Introduction
To justify:
Reason for other analogs introduced to inhibit other, specific reactions of the cycle.
Introduction:
Malonate is a succinate analog; it can also be introduced as another analog. It can also act as an inhibitor of the enzyme fumarase.
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
Malonate competes with succinate in the succinate dehydrogenase reaction. Explain why increasing the oxaloacetate concentration can overcome malonate inhibition.
When regulating phosphofructokinase, why is there such extensive regulation of this reaction and enzymatic reactions, in general?
One of the regulators of the TCA cycle is succinyl CoA. Discuss the rationale for this molecule to be used to regulate the TCA cycle [include chemical structures and chemical equations where appropriate].
What is an allosteric inhibitor? How does it operate?
For what TCA enzymes does succinyl CoA act as an inhibitor?
What is the metabolic role of succinyl CoA?
So then why is this molecule a reasonable choice as an inhibitor of the TCA?
Chapter 19 Solutions
Biochemistry
Ch. 19 - Radiolabeling with 14C-Glutamate Describe the...Ch. 19 - Prob. 2PCh. 19 - Assessing the Effect of Active-Site...Ch. 19 - Understanding the Mechanism of the -Ketoglutarate...Ch. 19 - Understanding the Action of Fluoroacetate on the...Ch. 19 - Prob. 6PCh. 19 - Prob. 7PCh. 19 - Prob. 8PCh. 19 - Prob. 9PCh. 19 - Prob. 10P
Ch. 19 - Prob. 11PCh. 19 - Prob. 12PCh. 19 - Prob. 13PCh. 19 - Prob. 14PCh. 19 - Prob. 15PCh. 19 - Prob. 16PCh. 19 - Understanding the Oxidation of Glucose and Its...Ch. 19 - Prob. 18PCh. 19 - Prob. 19PCh. 19 - Prob. 20PCh. 19 - Complete oxidation of a 16-carbon fatty acid can...Ch. 19 - Study Figure 19.18 and decide which of the...Ch. 19 - Prob. 23P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.arrow_forwardBased on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.arrow_forwardBased on the action of thiamine pyrophosphate in catalysis of the pyruvate dehydrogenase reaction, suggest a suitable mechanism for the fourth step in the pyruvate decarboxylase reaction in yeast:arrow_forward
- One of the regulators of the TCA cycle is succinyl CoA. Discuss the rationale for this molecule to be used to regulate the TCA cycle. For what TCA enzymes does succinyl CoA act as an inhibitor?arrow_forwardMalonate is a competitive inhibitor of succinate dehydrogenase. How will the concentrations of citric acid cycle intermediates change immediately after the addition of malonate? Why is malonate not a substrate for succinate dehydrogenase?arrow_forwardcan you explain the catalytic mechanism of pyruvate dehydrogenase (complex)arrow_forward
- Consider the mechanism of the aldolase reaction given in figure 9.25. In chapter 12, we saw that the same enzyme was used to catalyze the reverse reaction, DHAP + glyceraldehyde-3-phosphatefructose-1,6-bisphosphate, in the first step of stage 3 in the Calvin Cycle. Using arrows and structures similar to what is shown in 9.25, propose a mechanism for this reverse reaction (which is an aldol condensationarrow_forwardIodoacetate reacts irreversibly with the free -SH groups of cysteine residues in proteins. List which Calvin cycle enzyme(s) you would predict to be inhibited by iodoacetate, and briefly explain whyarrow_forwardThe catalytic efficiency of many enzymes depends on pH. Chymotrypsin, which has a well-known catalytic mechanism, shows a maximum value of kcat/Km at pH 8.0. A) Draw a pH curve of chymotrypsin activity over the pH range of 5 to 10 and briefly explain the rationale within the context of catalysis for your depiction. In particular, note how kcat and Km may change over this pH range. B) Enzymes of the a-amylase family catalyze a reaction by forming a covalent intermediate analogous to chymotrypsin, but to a conserved aspartate residue. Illustrate a catalytic mechanism containing a tetrahedral intermediate for a glycogen debranching enzyme based upon its potential membership in the a-amylase family. (don’t need to draw a whole glycogen)arrow_forward
- Demerol (meperidine) is a drug used to relieve moderate to severe pain through inhibition of theNADH dehydrogenase complex. Explain why this drug does not completely abolish oxidative phosphorylation.arrow_forwardPLP can catalyze both \alpha, \beta elimination reactions and \beta, \gamma - elimination reactions. Propose a mechanism for the following PLP - catalyzed \beta, \gamma eliminationarrow_forwardPhosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because itmimics the two physiological substrates of the enzyme. However, in the presence of substrates, lowconcentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.arrow_forward
arrow_back_ios
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY