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 11P
The following data describe the catalysis of cleavage of peptide bonds small peptides by the enzyme elastase.
The arrow indicates the peptide bond cleaved each case.
a. If a mixture of these three substrates was presented to elastase with the concentration of each peptide equal to 0.5 mM, which would be digested most rapidly? Which most slowly? (Assume enzyme present in excess.)
b. On basis of these data, suggest what features of amino acid sequence dictate the specificity of proteolytic cleavage by elastase.
c. Elastase is closely related to chymotrypsin. Suggest two kinds of amino acid residues you might expect to find in or near the active site.
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The following data describe the catalysis of cleavage of peptide bonds in
small peptides by the enzyme elastase.
Substrate
Ka(mM) ka(s")
PAPAIG
4.0
26
PAPA JA
1.5
37
PAPA ĮF
0.64
18
The arrow indicates the peptide bond cleaved in each case.
(a) If a mixture of these three substrates was presented to elastase with the
concentration of each peptide equal to 0.5 mm, which would be digested
most rapidly? Which most slowly? (Assume enzyme is present in excess.)
(b) On the basis of these data, suggest what features of amino acid sequence
dictate the specificity of proteolytic cleavage by elastase.
(c) Elastase is closely related to chymotrypsin. Suggest two kinds of amino
acid residues you might expect to find in or near the active site.
The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme
UTSASE (the arrow indicates the peptide bond cleaved in each case).
Substrate
Km(mM)
kcat(s)
PAPALG
4.0
26
РАPАLA
1.5
37
РАРАLF
0.64
18
Based on the above data shown for UTSAse what features of amino acid sequence dictate the specificity of
the proteolytic cleavage?
A. Large hydrophilic R-groups
B. Large hydrophobic R-groups
C. Neutral R-groups
D. Small hydrophilic R-groups
E. Large hydrophobic R-groups
F. Negatively charged R-groups
G. Positively charged R-groups
The following data describe the catalysis of cleavage of peptide bonds insmall peptides by the enzyme elastase. The arrow indicates the peptide bond cleaved in each case.(a) If a mixture of these three substrates was presented to elastase withthe concentration of each peptide equal to 0.5 mM, which would bedigested most rapidly? Which most slowly? (Assume enzyme is presentin excess.)(b) On the basis of these data, suggest what features of amino acid sequence dictate the specificity of proteolytic cleavage by elastase.(c) Elastase is closely related to chymotrypsin. Suggest two kinds of aminoacid residues you might expect to find in or near the 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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