Human Physiology
15th Edition
ISBN: 9781259864629
Author: Fox, Stuart Ira
Publisher: Mcgraw-hill Education,
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Chapter 4, Problem 5bCP
Summary Introduction
To review:
The end product inhibition and its effect on the concentration of different intermediates.
Introduction:
The sequence of enzymatic reactions, that begins with the initial substrate and the number of intermediates get involved in between the reaction to form the final product, is known as the
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Consider two enzymes catalyzing two reactions (A --> B --> C ) in a metabolic
cascade with their properties summarized below:
Keg (for
reaction)
Enzyme
Reaction
KM
Kcat / KM
102 M-1s-1
108 M-1s-1
1
A --> B
1
1 mM
2
B --> C
10
10 mM
Initial concentrations are [A] = 0.1 mM and [B] = [C] = 0 and both enzymes are
present at concentrations of 1 mM.
After waiting for 1 ms, the concentrations of A, B, and C are measured.
How do you expect the concentrations to be ordered?
O [B] > [A] > [C]
O [C] > [B] > [A]
O [A] > [B] > [C]
O [A] > [C] > [B]
[C] > [A] > [B]
In enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher (or raised) compared to the uncatalyzed reaction. List 4 factors that contribute to this raised energy level and explain how each of these factors contribute to the higher energy level of the ES complex
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.
Chapter 4 Solutions
Human Physiology
Ch. 4 - Use the lock-and-key model to explain how enzymes...Ch. 4 - Explain how enzymes are named, and the nature of...Ch. 4 - Draw graphs to represent the effects of changes in...Ch. 4 - Prob. 4CPCh. 4 - Prob. 5aCPCh. 4 - Prob. 5bCPCh. 4 - Prob. 5cCPCh. 4 - Prob. 6aCPCh. 4 - Define the terms exergonic reaction and endergonic...Ch. 4 - Prob. 7aCP
Ch. 4 - Prob. 7bCPCh. 4 - Which of these statements about enzymes is...Ch. 4 - Which of these statements about enzyme-catalyzed...Ch. 4 - Which of these statements about lactate...Ch. 4 - In a metabolic pathway, a. the product of one...Ch. 4 - In an inborn error of metabolism,
a. a genetic...Ch. 4 - Which of these represents an endergonic...Ch. 4 - Which of these statements about ATP is true? a....Ch. 4 - When oxygen is combined with 2 hydrogens to make...Ch. 4 - Enzymes increase the rate of chemical reactions...Ch. 4 - According to the law of mass action, which of...Ch. 4 - Explain the relationship between an enzyme's...Ch. 4 - Explain how the rate of enzymatic reactions may be...Ch. 4 - Explain how end-product inhibition represents a...Ch. 4 - Prob. 14RACh. 4 - The coenzymes NAD and FAD can "shuttle" hydrogens...Ch. 4 - Prob. 16RACh. 4 - Why do we need to eat food containing niacin and...Ch. 4 - Metabolic pathways can be likened to intersecting...Ch. 4 - Prob. 19RACh. 4 - Suppose you come across a bottle of enzyme tablets...Ch. 4 - Describe the energy transformations that occur...Ch. 4 - Use the reversible reactions involving the...Ch. 4 - Use the graph here and in figure 4.4 to answer the...Ch. 4 - Use the graph here and in figure 4.4 to answer the...Ch. 4 - Prob. 25RACh. 4 - Prob. 26RACh. 4 - Prob. 27RA
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- Using enzyme kinetics, illustrate the cooperative behavior of allosteric enzymes (plot of reaction velocity versus substrate concentration for instance)arrow_forwardSketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate delta delta G〒 on your sketch: Chemical step is rate limitingarrow_forwardcreate a single illustration that will interrelate or link the two opposing pathways, the Glycogenesis and Glycogenolysis. I want you to include the enzyme in each step and include some important by-products as well. From the illustration, I want you to encircle the intermediate molecule to highlight the link between the two processes. Aside from the illustration, I want you to compare and contrast the two pathways in terms of function, number of reaction steps, and usage of UTP. You can tabulate this part to make it simpler.arrow_forward
- Describe the two models that explain the behavior of allosteric enzymes. Include thelimitation or advantage of each. Give also an example of each.arrow_forwardPlease note the reaction expression below. Which of the following rate constants describes the breakdown of the enzyme-substrate complex? There may be more than one answer. k₂ E+S OK-2 U k₂ 0 k₁ OK.1 k3 k.3 SES EPE+P K.3 K.₂ k.arrow_forwarde) Two 20th century scientists, Leonor Michaelis and Maud Leonora Menten, proposed the model known as Michaelis-Menten Kinetics to account enzymatic dynamics. The model serves to explain how an enzyme can cause kinetic rate enhancement of a reaction and explains how reaction rates depends on the concentration of enzyme and substrate. k1 k2 E + S= ES → E + P k-1 Equation 1 i. Prove Equation 2 by referring to Equation 1. Vmax[S] V = [S] + KM Equation 2 ii. Give three characteristic features of catalyst.arrow_forward
- The figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?arrow_forwardIntermediates of a pathway are shown in the following scheme. Using curved arrows, show the mechanism of each step labeled with a blue letter. Draw out abbreviated structures of the coenzymes, so that you can effectively show all arrow pushing. You may abbreviate the coenzymes by putting R groups on the molecule, but do draw out the parts of the structure that are involved in the arrow pushing. Some of the transformations will require you to show multiple structures to show all of the arrow pushing (particularly some of the coenzyme-mediated steps). You do not need to show specific amino acid residues that perform the catalysis. You can abbreviate acidic amino acid residues “Enz–B–H” and basic residues “B–Enz”.arrow_forwardDescribe the specific multi-enzyme example discussed in class of how enzyme activity can be altered by changing its substrate to product ratio.arrow_forward
- When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?arrow_forwardOne way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000 How many molecules of urea can one molecule of urease act on in 12.0 min ?arrow_forwardHere’s a kinetic model for some enzyme E acting on substrate S. Give the equation for the change in the concentration of free enzyme (E) with time.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License