Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Chapter 12, Problem 12P
Interpretation Introduction
Interpretation:
Whether a
Concept introduction:
The alanine is a hydrophobic amino acid which forms intrachain hydrogen bond. Helix is formed in the hydrophobic medium, not in the liquid environment. If the helix is not formed there is no need to form intrachain.
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Examine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript.
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e4
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B
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e6
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F
Which enzymes catalyze irreversible reactions?
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Which of the enzymes is likely to be the allosteric
enzyme that controls the synthesis of G?
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e4
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26
5
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An allosteric enzyme that follows the concerted model has an allosteric coefficient (T/R) of 300 in the absence of substrate.
Suppose that a mutation reversed the ratio.
Select the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate
concentration, [S].
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The enzyme would likely follow Michaelis-Menten kinetics.
The plot of V versus [S] would be sigmoidal.
The enzyme would mostly be in the T form.
The plot of V versus [S] would be hyperbolic.
The enzyme would be more active.
Penicillin is hydrolyzed and thereby rendered inactive by penicillinase (also
known as ẞ-lactamase), an enzyme present in some penicillin-resistant
bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kDa.
The amount of penicillin hydrolyzed in 1 minute in a 10.0 mL. solution
containing 1.00 x 10 g 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.
Plots of V versus [S] and 1/V versus 1/[S] for these data are shown.
Vo (* 10 M minute"¹)
7.0
6.0
5.0
4.0
3.0
20
1.0
0.0
о
10
20
30
1/Vo (* 10 M1 minute)
20
103
90
BO
70
50
[S] (* 100 M)
40
50
60
y=762x+1.46 × 10"
[Penicillin] (M)
Amount hydrolyzed (uM)
1
0.11
3
0.25
5
0.34
10
0.45
30
0.58
50
0.61
Chapter 12 Solutions
Biochemistry (Looseleaf)
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