BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Chapter 32, Problem 14P
Interpretation Introduction
Interpretation:
The dissociation constant of lambda repressor-DNA complex and standard free energy of binding should be determined.
Concept introduction:
Theλ repressor in activated state binds to OR1 and OR2 sites and inhibits the transcription of phage gene. On the other hand, Cro protein binds to the same sites, to which λ repressor binds. In this way, the Cro protein inhibits the action of λ repressor.
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The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S.
b
Question Content Area
The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1.
Calculate the catalytic efficiency with S, T, and U.
Catalytic efficiency with S =
Catalytic efficiency with T =
Catalytic efficiency with U =
Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?
Fumerase catalyzes the conversion of fumerate to malate.
fumerate + H2O ⇋ malate
The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1.
a
In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?
Suppose you wanted to make a buffer of exactly pH 7.00 using KH2PO4 and Na2HPO4. If the final solution was 0.18 M in KH2PO4, you would need 0.25 M Na2HPO4. Now assume you wish to make a buffer at the same pH, using the same substances, but want the total phosphate molarity ([HPO42−]+[H2PO−4]) to equal 0.20 M. What concentration of the Na2HPO4 would be required?
Chapter 32 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
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