Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Chapter 12, Problem 10P
Interpretation Introduction
Interpretation:
The reason for the glycosylated lipids to be lesslikely to flip-flop needs to be explained.
ConceptIntroduction:
In addition to galactose, they start an energy barrier to flip-flop. This energetic barrier improvesthe irregularity of the membrane. The addition of carbohydrates significant energy barrier to the flip-flop.
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Examine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript.
e₁
e3
e4
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B
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e5
e6
e7
E
F
Which enzymes catalyze irreversible reactions?
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e4
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es
26
5
e7
Which of the enzymes is likely to be the allosteric
enzyme that controls the synthesis of G?
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e4
es
26
5
e7
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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