The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a 3. few sentences. mOH pe0 p oSH) d ls sw. (asae (a) H notase ors vol woind sidst no nbe sd tiw ps er mundiaps ueeg bus TH Eseo.o 888.0 4. Consider the following reaction, which is exothermic: 5.0 SEO O C2H4 (g) + Br2 (g) → C2H¾Br2 (g) ΔΗ 0 Predict the effect of each of the following perturbations (shift right/products, shift left/reactants, or no effect) using Le Chatelier's principle a. The reaction temperature is increased: b. The reaction volume is decreased: C. More bromine gas is added: d. The reaction is done in the presence of helium: e. C2H4BR2 is removed from the reaction vessel as it is being produced: f. The reaction is done in an ice bath instead of at room temperature: g. The reaction is done in the presence of a catalyst: nisloa Snodse1 pimisdioxa 1o almedtobns ns airlt al b

The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a 3. few sentences. mOH pe0 p oSH) d ls sw. (asae (a) H notase ors vol woind sidst no nbe sd tiw ps er mundiaps ueeg bus TH Eseo.o 888.0 4. Consider the following reaction, which is exothermic: 5.0 SEO O C2H4 (g) + Br2 (g) → C2H¾Br2 (g) ΔΗ 0 Predict the effect of each of the following perturbations (shift right/products, shift left/reactants, or no effect) using Le Chatelier's principle a. The reaction temperature is increased: b. The reaction volume is decreased: C. More bromine gas is added: d. The reaction is done in the presence of helium: e. C2H4BR2 is removed from the reaction vessel as it is being produced: f. The reaction is done in an ice bath instead of at room temperature: g. The reaction is done in the presence of a catalyst: nisloa Snodse1 pimisdioxa 1o almedtobns ns airlt al b

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. D= V [S] K+|S| where is the velocity, or rate, V is the maximum velocity, K., is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (,) at different substrate concentrations ([S]). First, move the line labeled Vaux to a position that represents the maximum velocity of the enzyme. 300 Next, move the line labeled 1/2 V to its correct position. Then, move the line labeled K, to its correct position. 275 250 1/2 V Estimate the values for V and Km. V= μM/min •M/min) 200 175 150 125 010 R 4050 (M) 8. Michaelis-Menten curve R 8. B M 100
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Q8. Please define the terms of adsorption, adsorbate, adsorbent and draw the figure of adsorption of a chemical on an adsorbent surface.
Our body obtains energy from the combustion of glucose. During this process, glycerate is transformed first into pyruvate. This reaction has an activation energy close to 44 kJ. Estimate how many times faster this reaction is when someone has a high fever close to 106 F (41 oC) compared to its rate at normal body temperature (98.6 F; 37 oC). Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a b с d 31% faster 11% faster 24% faster 259% faster Your answer
Rate Enhancement by Urease.The enzyme urease enhances the rate of urea hydrolysis at pH 8.0 and 20 °C by a factor of 1014. If a given quantity of urease can completely hydrolyze a given quantity of urea in 5.0 min at 20 °C and pH 8.0, how long would it take for this amount of urea to be hydrolyzed under the same conditions in the absence of urease? Assume that both reactions take place in sterile systems so that bacteria cannot attack the urea.
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