Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 2P
The enzyme urease catalyzes the hydrolysis of urea to ammonia plus carbon dioxide. At 210C the uncatalyzed reaction has an activation energy of about 125 kJ/mol, whereas in the presence of urease the activation energy is lowered to about 46 kJ/mol. By what factor does urease increase the velocity of the reaction?
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Urease enzyme hydrolysed urea at [S]= 0.03
mmol/L with a Km value of around 0.06
mmol/L. The initial velocity observed was
1.5x103 mmol/L.min1. Calculate the initial
velocity of the enzymatic reaction when using
[S]= 0.12 mmol/L.
The enzyme urease increases the rate of urea hydrolysis at pH 8.0 and 20 °C by a factor of 10^14. Suppose that a given quantity of urease can completely hydrolyze a given quantity of urea in 10 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 in sterile conditions?
The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3
Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
Chapter 8 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 8 - Prob. 1PCh. 8 - The enzyme urease catalyzes the hydrolysis of urea...Ch. 8 - An enzyme contains an active site aspartic acid...Ch. 8 - The folding and unfolding rate constants for a...Ch. 8 - In some reactions, in which a protein molecule is...Ch. 8 - Would you expect an “enzyme” designed to bind to...Ch. 8 - The initial rate for an enzyme-catalyzed reaction...Ch. 8 - a. If the total enzyme concentration in Problem 7...Ch. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - The following data describe the catalysis of...Ch. 8 - At 37 oC, the serine protease subtilisin has kcat...Ch. 8 - The accompanying figure shows three...Ch. 8 - The steady-state kinetics of an enzyme are studied...Ch. 8 - The same enzyme as in Problem 14 is studied in the...Ch. 8 - Enalapril is an anti-hypertension “pro-drug"...Ch. 8 - Initial rate data for an enzyme that obeys...Ch. 8 - Prob. 18PCh. 8 - Suggest the effects of each of the following...Ch. 8 - The inhibitory effect of an uncompetitive...Ch. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - In kinetics experiments, the hydrolysis of the...
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- there are A-D questions to this picture set up. A) What enzyme catalyzes this reaction? B) What is Delta G, please answer in Joules, K=19 C) If concentration of Glucose-1_Phosphate is 48.82 uM at equalibrium, what is the concentration of Glucose-6-phosphate in uM? D) If the reaction is NOT at equalibrium, what is delta G at 25C if the concentration of Glucose-1-phosphate is 15.04 uM and concentration of Glucose -6-phosphate is 1.62 mM? please answer in Joules and in significant figures. *note, 10^3uM in 1 mM Thank you!!arrow_forwardA bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 m mol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM?arrow_forwardAn enzyme has a single active site at which it can bind and hydrolyze either X or Y; however, the enzyme cannot bind X and Y at the same time. Answer the following questions regarding the Km and Vmax of this enzyme. (a) Will the Km for X be affected if Y is present in the reaction mixture? Explain. (b) Will Vmax for X be affected if Y is present in the reaction mixture? Explain. (a) No, X competes with Y for binding, so the apparent Km for X will stay the same. (b) Yes, the Vmax for X will decrease in the presence of Y. (a) No, Y does not compete with X for binding, so the apparent Km for X will stay the same. (b) No, the Vmax for X will be unaffected by the presence of Y.arrow_forward
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