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The KM is: equal to the substrate concentration when the reaction rate is half
its maximal value.
6. What conclusion can be drawn concerning an inhibitor if the Vmax is the same in
the presence and absence of the inhibitor? The inhibitor can be overcome with
sufficiently high concentrations of substrate.
11. What factor(s) influence(s) the binding of oxygen to myoglobin? The partial
pressure of oxygen, pO2
12. Which of the following is true under the following conditions: The enzyme
concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 M? The
enzyme is saturated with substrate.
13. Carbon dioxide forms carbamate groups in proteins by reaction with: N-terminal
amino groups.
14. The Gibbs-free energy of activation is: the difference between the substrate
and the transition state.
16. Sickle-cell anemia is caused by: a substitution of a Val residue for a Glu
residue at the 6 position.
18. What is the Bohr effect? the regulation of hemoglobin-binding by hydrogen ions
and carbon dioxide
19. The energy that is released by the hydrolysis of ATP by actin is used for:
actin filament assembly.
20. Which of the following parts of the IgG molecule are not involved in binding to
an antigen? Fc
22. In a plot of l/V against 1/[S] for an enzyme-catalyzed reaction, the presence
of a competitive inhibitor will alter the: intercept on the l/[S] axis.
23. When substrate concentration is much greater than KM, the rate of catalysis is
almost equal to: Vmax
24. Both water and glucose share an -OH that can serve as a substrate for a
reaction with the terminal phosphate of ATP catalyzed by hexokinase. Glucose,
however, is about a million times more reactive as a substrate than water. The
best explanation is that: the larger glucose binds better to the enzyme; it induces
a conformational change in hexokinase that brings active-site amino acids into
position for catalysis.
27. A and B interact with Kd = 10^-8 M; A and C interact with Kd = 10^-7 M. What
does this tell you about A, B, and C? The interaction affinity between A and B is
higher than that between A and C.
28. Which of the following is the most accurate statement regarding the enzyme
chymotrypsin? The catalytic mechanism of chymotrypsin involves a catalytic triad
composed of an aspartate, a histidine, and a serine residue.
29. A good transition-state analog: binds to the enzyme more tightly than the
substrate.
30. The rate of breakdown of the enzyme-substrate complex can be described by the
expression: k-1 [ES] + k2 [ES].