The catalytic activity of enzymes depends on the presence of appropriate environmentalconditions. Pepsin is a digestive enzyme found in the stomach and facilitates the digestionof large proteins.If pepsin is removed from this acidic environment of the stomach and is instead placed ina more basic environment, it will cease to function. Describe the specific effect that achange in environmental pH will have on pepsin and explain how this change can lead toinhibition of its catalytic activity.Respond in 4 to 6 complete sentences.

Pepsin is a digestive enzyme found in the stomach. It is a type of hydrolase enzyme that help in…

Answered: The catalytic activity of enzymes…

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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Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.
Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.
Glucose can be isomerized to fructose to glucose isomerase. The enzyme kinetics of this enzyme was studied in the presence of an inhibitor X. Using the data provided, complete the table and determine what type of inhibitor is X. 1/ [S] , 1/M 1/V, w/o inhibitor Min/M 0.22 1/V, w/ inhibitor 0.33 0.27 0.2 0.16 0.20 0.14 0.13 0.16 0.11 0.11 0.14 0.09 0.11 0.13 Km/Vmax 1/Vmax Km Vmax
The change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the table below. Determine the Vmax and Km of the enzyme in the absence and presence of C. Is C an inhibitor or an activator of enzyme A? Determine the type of inhibition or activation. Rate of formation of Product B in the presence of 25 mg/mL C (mM/min) Substrate Rate of formation of (mM) Product B (mM/min) 0.5 21.5 14.1 1 30.2 22.2 1.5 34.9 27.0 2.5 39.8 33.1 3.5 42.0 36.3
Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
Consider the following enzyme cartoons or structures carefully. Note active sites, presence of cofactors, substrates, etc. and then answer the following questions with the applicable numbers 1, 2, 3, 4, None or All. More than one number may apply. 3. 2. 1. GO Substrate Enzyme Substrate Enzyme Pepsin Enolase a. Example(s) of an allosteric enzyme b. Example(s) of a proteolytic enzyme c. Example(s) of an enzyme(s) with cofactor(s) e. Example(s) of an enzyme(s) that could be impacted by an irreversible competitor. d. Example(s) of an enzyme(s) with a second site for feedback control. f. Enzyme(s) definitely composed of two or more protein chains.
Because it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?
Consider the Michaelis-Menten equation, below: Vmaz (S V. k + [S] %3D What is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7 The S terms cancel out in this equation, so there is no effect of changing substrate concentration. The S] term in the numerator is negligible, so there is no impact of changing substrate concentration. Because the enzyme has reached Vr there is no effect of changing substrate concentrations on enzyme velocity. OThe [S term in the denominator is negligible compared to k There is a linear relationship between substrate concentration and velocity.
Write Cifonly statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. When an inhibitor binds to the enzyme-substrate complex, the inhibition mode is uncompetitive. B. As a consequence, the enzyme's efficiency is decreased along with the maximum velocity.
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
The catalytic efficiency of many enzymes depends on pH. Chymotrypsin shows a maximum value of kaKM at pH 8. Detailed analysis shows that kat increases rapidly between pH 6 and 7 and remains constant at higher pH. KM increases rapidly between pH 8 and 10. Suggest explanations for these observations.
In the Lineweaver Burke plot shown below, which of the following is true? With inbito Wthout nhitor O Km is increasing. Vmax is decreasing Km is decreasing, Vmax is decreasing Km is increasing, Vmax is increasing Km is decreasing, Vmax is in QUESTION 35 As per the Enzyme commission classification, the tranferases belong to which of the following Class? O 2 O 4 O 3 Click Save and Submit to save and submit. Click Save All Answers to save all answers. 78 F Mostly cloudy

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