Use the following information to answer the question(s) below. A series of enzymes catalyze the reaction X→Y→ Z → A. Product A binds to the enzyme that converts X to Y at a position remote from its active site. This binding decreases the activity of the enzyme. With respect to the enzyme that converts X to Y, substance A functions as an allosteric inhibitor a competitive inhibitor the substrate an intermediate a coenzyme

Use the following information to answer the question(s) below. A series of enzymes catalyze the reaction X→Y→ Z → A. Product A binds to the enzyme that converts X to Y at a position remote from its active site. This binding decreases the activity of the enzyme. With respect to the enzyme that converts X to Y, substance A functions as an allosteric inhibitor a competitive inhibitor the substrate an intermediate a coenzyme

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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A competitive inhibitor competes with substrate for binding to the active site of the enzyme. The enzyme, once bound by the inhibitor, is unable to form product. How would a competitive inhibitor affect the velocity of product formation? Would you need more or less of the substrate to get the same velocity as found before the inhibitor was added?
Fill in the blanks and answer the question: A. The enzyme ATCase (aspartate transcarbamoylase) uses _________________control to regulate its activity. The molecule ATP is an allosteric _____________ of ATCase and because it is a molecule different from the substrate of this enzyme it produces an _________________ effect in the enzyme’s activity. B. Is it appropriate to study the enzymatic activity of ATCase with the Michaelis Menten approximation? Justify your answer.
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
The effect of on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y) an allosteric effector a noncompetitive inhibitor a competitive inhibitor
What are the steps for an enzyme to create a product in order: The energy of activation is lowered so the reaction can happen quicker. Substrate attaches to the active site. The product is created and released from the active site. The energy of activation is lowered so the reaction can happen slower. A specific substrate attaches to the active site.
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
You are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?
41) Use the following information to answer the 2 questions below. C. b. A+B a. d. ,C+D Progress of the Reaction The figure illustrates the energy states associated with the reaction A +B -C+ D. Which of the following represents the activation energy required for the enzyme-catalyzed reaction in the figure? A) a B) b C) c D) d Free Energy
Which of the following is NOT a true statement about the diagram below? Intermediate A Intermediate B End-product Pathway operates 2019 Pearson Education, Inc. O O O O Substrate Enzyme 1- Allosteric site -Enzyme 2 Enzyme 3- Pathway shuts down Bound end-product Feedback Inhibition The end-product None of the other four answers (all are true statements) Each enzyme is specific for its substrate The product of each enzyme reaction becomes a substrate for the next enzyme The diagram shows a metabolic pathway serves as a competitive inhibitor of the substrate on Enzyme 1
Discuss the following statement: “enzymes and heat are alike in that both can speed up reactions that—although thermodynamically feasible—do not occur at an appreciable rate because they require a high activation energy. diseases that seem to benefit from the careful application of heat—in the form of hot chicken soup, for example—are therefore likely to be due to the insufficient function of an enzyme.”