BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
1st Edition
ISBN: 9780134172507
Author: APPLING
Publisher: Pearson Education
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Chapter 8, Problem 10P
Interpretation Introduction
Interpretation:
The explanation for the observation that kcat increases rapidly between pH 6 and 7 and remains constant at higher pH. Km also increases rapidly between pH 8 and 10 should be determined.
Concept introduction:
The pH is the main factor to decide the activity of an enzyme moreover at optimum pH the activity of the enzyme is maximum which indicates that it is converting more and more substrate to product.
The activity of the enzyme can be determined through Kcat/KM, higher the value of Kcat give the maximum activity of the enzyme and this activity lowers down with a decrease in value of Kcat.
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Chapter 8 Solutions
BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
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. 21P
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