The enzyme urease increases the rate of urea hydrolysis at pH 8.0 and 20 °C by a factor of 1014.Suppose that a given quantity of urease can completely hydrolyze a given quantity of urea in 19 minutes at pH 8.0 and 20 °C.How long would it take for this amount of urea to be hydrolyzed in the absence of urease at the same temperature and pH insterile conditions? Include two significant figures in your answer.timeuncatalyzedyears* TOOLSx10

Given that : At pH 8.0 and 20°C, the enzyme urease increases the rate of urea hydrolysis by a factor…

Answered: The enzyme urease increases the rate of…

Chemistry: The Molecular Science

5th Edition

ISBN:9781285199047

Author:John W. Moore, Conrad L. Stanitski

Publisher:John W. Moore, Conrad L. Stanitski

Chapter11: Chemical Kinetics: Rates Of Reactions

Section: Chapter Questions

Problem 83QRT

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List two ways that enzyme catalysis of a reaction is superior to normal conditions.
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
Glycolysis is the process by which glucose is metabolized to lactic acid according to the equation C6H12O6(aq)2C3H6O3(aq) G=198 kJ at pH 7.0 and 25°C Glycolysis is the source of energy in human red blood cells. In these cells, the concentration of glucose is 5.0103 M, while that of lactic acid is 2.9103 M. Calculate AG for glycolysis in human blood cells under these conditions. Use the equation G=G+RT In Q, where Q is the concentration quotient, analogous to K.
The enzyme urease increases the rate of urea hydrolysis at pH 8.0pH 8.0 and 20 °C20 °C by a factor of 1014.1014. Suppose that a given quantity of urease can completely hydrolyze a given quantity of urea in 88 minutes at pH 8.0pH 8.0 and 20 °C.20 °C. How long would it take for this amount of urea to be hydrolyzed in the absence of urease at the same temperature and pH in sterile conditions? how many years?
Distinguish between mixed-acid fermentation and butanediol fermentation and describe the test(s) that can be used to detect each. Briefly describe the reactions and changes that take place during the decarboxylation of amino acids in the decarboxylase medium. Explain the experiment that you would perform in order to determine whether the organism that you were instructed instructed to identify is positive or negative for gelatin hydrolysis. How do microorganisms such as bacteria eliminate harmful reactive oxygen species? Nitrate reduction to nitrite is indicated by the formation of a pink to red color after addition of nitrate test reagent. However, if a culture does not produce a colour change several possibilities exist. Explain.
1. Penicillin is hydrolyzed and thereby rendered inactive penicillinase, an enzyme present in some penicillin-resistant bacteria. The molecular weight of this enzyme in Staphylococcus aureus is 29.6 kilo Daltons (29.6 kg/mole or 29,600 g/mole or 29,600 ng/nmole) The amount of penicillin hydrolyzed in 2 minute in a 10-mL solution containing 109 g (1 ng) of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. [Hint: Convert everything to the same concentration terms] Show all calculations and include spreadsheets and graphs to determine Km, Vmax and kcat for this enzyme. Make sure your final answers have correct units. [Another hint: Note that [S] and amount hydrolyzed are already in concentration terms. So you don't need to worry about the volume for calculating [S] and V. ] Penicillin concentration (microM) Amount hydrolyzed (nanoM) 1 110 3 250 5 340 10 450 30 580…
- Vegetable oils are typically liquid at room temperature, yet Crisco (which is made of vegetable oil) is solid at room temperature. Explain why/how this is the case. - Explain, with the use of a diagram how soap molecules work to clean “dirt” particles. - Amylase is a natural enzyme found in saliva. Describe this enzyme’s function. - Lactose is a sugar found in milk and other dairy products. Explain how it is broken down in most individuals. Explain lactose “intolerance”.
Which statement does NOT apply to the lock-and-key theory? O explains the functioning of enzymes explains the need for a specific three dimensional structure found in proteins explains the reason why a particular enzyme is involved with one substrate explains why a substrate-enzyme complex is so difficult to separate
An enzyme requires a Zn2+ ion in order to function correctly. In this case, the Zn2+ is a(n) a. apoenzyme b. coenzyme c. cofactor d. subunit 24. A substance that can bind to an enzyme at a location other than the active site and increase or decrease the activity of that enzyme is called a(n) a. subunit b. proenzyme c. modulator d. feedback inhibitor
Enzymes function most efficiently at the temperature of a typical cell, which is 37 degrees Celsius. Increases or decreases in temperature can significantly lower the reaction rate. What does this suggest about the importance of temperature-regulating mechanisms in organisms? How does this translate to the development of enzyme assays for clinical laboratory testing equipment? Explain.
Substrate Enzyme-substrate complex 1. Is this an example of a lock & key or induced fit model of an enzyme? > Enzyme
The enzyme urease catalyzes the breakdown of urea in the body. Urease breaks urea down to 2NH3 + CO2. This is an example of a hydrolysis reaction (urea plus water For each equivalent of carbon dioxide (CO2), two equivalents of ammonia (NH3) are produced. Label the enzyme, substrate, enzyme-substrate complex, enzyme-product complex, and product in the enzymatic reaction for the breakdown of urea by urease using the induced-fit model. Drag the appropriate labels to their respective targets. ► View Available Hint(s) Urease – 2NH3 + CO2 Urea - 2NH3 + CO2 Urease - Urea 2NH3 + CO2 Urease Urea cj Complex Pearson 1. + Complex Reset Help

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