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.
Write the chemical equilibrium and expression for the equilibrium constants for the ionization of (a) tartaric acid. (b) malic acid.
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?
1. A daily low dosage of aspirin (acetylsalicylic acid) can lower the risk of heart attack and stroke for individuals at risk. Aspirin suppresses the generation of prostaglandins by irreversible binding to the enzyme COX-1. Inhibition of prostaglandin synthesis lowers the production of thromboxanes that are responsible for the aggregation of platelets and the formation of blood clots. You will explore the mechanism of aspirin binding. 1.1 The average pH of the human body is 7.4 (also known as a physiological pH). Draw the structure of aspirin at a physiological pH. OH 1.2 Aspirin reacts with the amino acid Serine. What is the structure of serine? Draw the structure of the tripeptide Ala-Ser-Trp (draw these structures as they exist at physiological pH) serine Ala-Ser-Trp 1.3 Aspirin reacts with Serine 530 of COX-1 by transesterification reaction. Draw a general mechanism of acid-catalyzed transesterification reaction. Use HA as an acid. 1.4 Draw an arrow-pushing mechanism for the…
Calculate the equilibrium constant for the phosphorylation of glucose to glucose 6-phosphate at 37.0 °C. K'eq = 4.74 x10-3 In the rat hepatocyte, the physiological concentrations of glucose and P₁ are maintained at approximately 4.8 mM. What is the equilibrium concentration of glucose 6-phosphate (G6P) obtained by the direct phosphorylation of glucose by P₁? [G6P]: 8.75 X10-8 M-1 Incorrect M
An 90 kg subject consumed a snack that contained 80 g of carbohydrate. Before eating the snack the subject’s blood glucose was 6.0 mmol.L-1. Calculate the concentration of glucose (mM) that would be reached in the blood after consuming the snack.Assume that all the carbohydrate in the snack was converted to glucose, rapidly absorbed and distributed throughout the extracellular water (ECW) within 30 minutes. Assume ECW is approximately 20% of body weight and the glucose is not metabolised further.
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Lactase is an enzyme that breaks down the sugar lactose which is commonly found in dairy products. Some people develop lactose intolerance as they grow older and the amount of lactase enzyme in their gut diminishes. Since the enzyme is commonly found in the gut of humans it can withstand a pH that is very acidic, ranging from a pH of 2-7. A student decided to do an experiment to determine how the pH of a solution affects lactase enzyme activity. Lactase works by breaking lactose into its two component sugars of glucose and galactose. To conduct the experiment the student prepared a solution of lactose and placed it into 5 different test tubes. A pH buffer solution was then added to each test tube with a pH of 2.0 in the first tube, 4.0 in the second, 6.0 in the third, 8.0 in the fourth, and a 10 pH in the fifth. Next, the enzyme lactase was added in equal amounts to each test tube and allowed to sit for ten minutes white the enzyme reacted with the lactose. At the end of the ten…
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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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