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Page 2
Which of the following graphs would explain why ethanol is an effective treatment for methanol poisoning.
13.
You want to choose something that is a competitive inhibitor so you want the Km to increase and Vmax to stay
constant
i.
Graph A
a.
Substrate concentrations
a.
All enzymes are regulated by
14.
Activate or deactivate an enzyme
a.
Introduce a negative charge and a covalent bond
b.
Phosphorylation of an enzyme will
15.
If you have an increase in Km- most likely
competitive inhibition
i.
The amino acid substitution likely occurs in the active site and affects electrostatic interactions
a.
Remember high Km means concentrations of acid aldehyde build up and you get drunk quicker
i.
Individuals with the genetic variant in ALDH@ do not metabolize alcohol very well
b.
What can u conclude from the data?
16.
Doubling [S] will not affect the K
m
or V
max
17.
Remember that salts can act as an uncompetitive inhibitor which affects both
a.
1 M NaCl will change both Km and Vmax
18.
Mixed noncompetitive inhibitor affect both Km and Vmax
19.
Competitive inhibitor will affect Km
20.
Noncompetitive inhibitor will affect Vmax
21.
The reaction for hydrolysis has a high activation energy
a.
The hydrolysis of ATP has a large negative delta G, however, the molecule is quite stable in solution. How can this be
explained?
22.
The first step in the metabolism of glucose involved the addition of a phosphate group catalyzed by the enzymes
hexokinase/glucokinase
23.
The following applies to enzymes that show M-M kinetics
Biochem Page 2
Page 3
-16.7 kJ/mol
a.
Favorable reactions release energy
a.
Favorable reactions increase entropy
b.
Favorable reactions have a negative delta G
c.
Which of the following determines whether a reaction is favorable?
24.
Measure of energy available to do work
a.
Depends on the concentrations of reactants and products
b.
Depends on the change in bond energy between reactants and products
c.
Delta G is dependent on Entropy
d.
The following question refers to delta G.
25.
They lower the activation energy of a reaction
a.
Which of the following statements applies to enzyme catalysts?
26.
The turnover number (kcat)
a.
The number of substrate converted to product per mole of enzyme in a given unit of time is defined as:
27.
Low Km is usually advantageious
i.
Aspargine-1
a.
Which of the following variants of asparagine in the table below would be the most effective?
28.
Enzymes are facinating macromolecules that may be required for certain reactions in the cell to proceed.
They can speed up
or slow down a reaction by changing its
Activation Energy
. Their action can also be regulated by inhibitors or activators.
In
competitive inhibition the inhibitor will bind to the
Active Site
of the enzyme, thereby modifying its ability to function
properly.
Pharmaceutical companies may take advantage of the fact that the
Transition state
always bind very tightly to the
enzyme and therefore design inhibitors of the enzyme to mimic this structure.
29.
Remember that delta G is not dependent on reaction rate.
Enzymes affect reaction rate
i.
-5.6
a.
30.
The transition state is stabilized by the enzyme but the bonds are strained
a.
A molecule that mimics the transition state binds to the enzyme more tightly
b.
A molecule that resembles the transition state may be an effective competitive inhibitor
c.
The higher the free energy difference between the substrate and the transition state, the slower the reaction
d.
The following statements refer to the transition state
31.
Stabilization of transition state
a.
What is the common strategy by which catalysis occurs?
32.
Doubling the enzyme concentration affects the V max
33.
Uncompetitive inhibitor decreases both Km and Vmax
34.
Biochem Page 3
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