Consider a biochemical reaction A to B, which is catalyzed by A-B dehydrogenase.
Which of the following statements is true?
A. The reaction will proceed until the enzyme concentration decreases.
B. The reaction will be more favorable at 0 degrees C.
C. A component of the enzyme transferred from A to B.
D. The free energy change (delta G) of the catalyzed reaction is the same as for the
uncatalyzed reaction. - Answer D.
-In an enzyme-catalyzed reaction, the rate of a reaction is increased by a decrease in
the activation energy. Furthermore, enzymes are not changed or consumed during the
course of the reaction. Also, the overall free energy change of the reaction, delta G,
remains unchanged in the presence of an enzyme.
Which of the following statements about enzyme kinetics is false?
A. An increase in the substrate concentration (at constant enzyme concentration) leads
to proportional increases in the rate of the reaction.
B. Most enzymes operating in the human body work best at a temperature of 37 degree
C.
C. An enzyme-substrate complex can either form a product or dissociate back into the
enzyme and substrate.
D. Maximal activity of many human enzymes occurs around pH 7.2. - Answer A.
-Most enzymes in the human body operate a maximal activity around a temperature of
37 degrees C and a pH of 7.2, which is the pH of most body fluids. In addition, as
characterized by the Michaelis-Menten model, enzymes form an enzyme-substrate
complex, which can either dissociate back into the enzyme and substrate or proceed to
form a product. We can eliminate B, C, and D. An increase in the substrate
concentration, while maintaining a constant enzyme concentration, leads to a
proportional increase in the rate of the reaction only initially. However, once most of the
active sites are occupied, the reaction rate levels off, regardless of further increases in
substrate concentration. At high concentrations of substrate, the reaction rate
approaches its maximal velocity and is no longer changed by further increases in
substrate concentration. Therefore statement A is not entirely true.
At which pH would pancreatic enzymes work at maximum activity?
A. 5.3
B. 6.7
C. 7.2
D. 8.5 - Answer D.
-Pancreatic enzymes work optimally in the alkaline condition of the small intestine. It is
not necessary to know the exact pH at which these enzymes work because the only
very basic pH is seen in (D), which is 8.5.
,Some enzymes require the presence of a non-protein molecule to behave catalytically.
An enzyme devoid of this molecule is called a(n):
A. holoenzyme
B. apoenzyme
C. coenzyme
D. zymoenzyme - Answer B.
-An enzyme devoid of its necessary cofactor is called an apo-enzyme and is
catalytically inactive.
Which of the following factors determine an enzyme's specificity?
A. The 3D shape of the active site.
B. The Michaelis constant.
C. The type of cofactor required for the enzyme to be active.
D. The prosthetic group on the enzyme. - Answer A.
-An enzyme's specificity is determined by the 3D shape of its active site. Regardless of
which theory of enzyme specificity we are discussing (lock and key or induced fit), the
active site determines which substrate the enzyme will react with.
Enzymes increase the rate of a reaction by:
A. decreasing the activation energy.
B. increasing the overall free energy of the reaction.
C. both A and B.
D. none of the above. - Answer A.
-Enzymes increase the rate of a reaction by decreasing the activation energy. They do
not affect the overall free energy, delta G, of the reaction.
Bonding between atoms of an enzyme such as trypsin is best described as:
A. peptide
B. saccharide
C. ionic
D. van der Waals - Answer A.
-Enzymes are proteins. Proteins are composed of amino acids linked together by
peptide bonds. Choice (B) - Saccharide, is a type of bond found in polysaccharides.
Choice (C) - Ionic, is a chemical bond formed through electrostatic interaction between
positive and negative ions. Choice (D) may be formed in secondary or tertiary structures
of an enzyme but is not as good an option as (A).
In the equation below, substrate C is an allosteric inhibitor to enzyme 1. Which of the
following is another mechanism caused by substrate C?
A --> enzyme 1 --> B --> enzyme 2 --> C.
,A. Competitive inhibition
B. Irreversible inhibition
C. Feedback enhancement
D. Negative feedback - Answer D.
-By limiting the activity of enzyme 1, the rest of the pathway is slowed, which is the
definition of negative feedback. Choice (A) is incorrect because there is no competition
for the active site with allosteric interactions. There is not enough information for (B) to
be correct because we aren't told whether the inhibition is reversible. In general,
allosteric interactions are temporary. Choice (C) is incorrect because is it the opposite of
what occurs when enzyme 1 activity is reduced.
When lactose hydrolyzes its substrate, lactose, which of the following occurs?
A. Lactase retains it structure after the reaction.
B. Lactose retains its structure after the reaction.
C. Lactase increases the activation energy of the reaction.
D. Lactose decreases the activation energy of the reaction. - Answer A.
-Choice (A) is correct answer because, by definition, an enzyme remains unchanged by
the reaction that is catalyzes. Choice (B) is incorrect because a substrate is changed by
an enzymatic reaction. Choice (C) is not true, an enzyme would decrease the activation
energy. Choice (D) is also incorrect since a substrate does not affect the activation
energy.
Discuss why competitive inhibition can be overcome with increasing substrate
concentration but non-competitive inhibition cannot be overcome. - Answer -Competitive
inhibitors are structurally similar to the substrate of an enzyme. This means that in the
course of catalyzing reactions the enzyme can bind the inhibitor instead of the
substrate. Imagine there are an equal number of inhibitor and substrate molecules. The
chance that the enzyme will bind the inhibitor is equal to the chance that it will interact
with the substrate. Thus, the rate of catalysis will be decreased, effectively inhibiting the
enzyme. However, if the concentration of substrate if 1,000 or 100,000 times greater
than the concentration of inhibitor, then the chance the enzyme will randomly interact
with the inhibitor instead of the substrate falls dramatically (practically to zero).
-Noncompetitive inhibitors do not associate with the enzyme at the active site. Instead,
they bind at an allosteric site. When a noncompetitive inhibitor is bound, the enzyme
cannot catalyze bind the substrate. Increasing the concentration of substrate will not
decrease the likelihood of a noncompetitive inhibitor associating at an allosteric site.
Why is negative feedback inhibition more common than positive feedback loops? Are
there biological examples when positive feedback is necessary? - Answer -Most
biological conditions, such as blood pH, body temperature, and blood pressure, must be
kept within a narrow range. Negative feedback allows for the maintenance of these
conditions. If a homeostatic system moves too far to one extreme, negative feedback
will brings the levels back within biologically acceptable conditions. Positive feedback,
, however, has the opposite effect. The more a process moves in a particular direction,
the more positive feedback will keep it moving in that same direction. Two examples in
which positive feedback is important are blood clotting and childbirth.
Compare and contrast the the concept of allosteric effectors with non-competitive
inhibition. - Answer -First, all noncompetitive inhibitors bind at allosteric sites. The
binding of noncompetitive inhibitors, however, does not affect the binding of substrate to
the active site (and vice versa). What noncompetitive inhibitors do affect is the ability for
the enzyme to catalyze the reaction and release product. In contrast, allosteric effectors
allow the enzyme to exist in two different confirmations (T and R), in which one state
binds substrate more readily than the other. Again, this is in direct contract to
noncompetitive inhibitors, which do not influence the binding of substrate.
Consider the pathway:
A --1-> B --2-> C --3-> D --4-> E
--5-> X --6-> Y
An increase in [E] leads to the inhibition of enzyme 3. All of the following are results of
the process except:
A. an increase in [B].
B. an increase in [Y}.
C. decreased activity of enzyme 4.
D. increased activity of enzyme 6. - Answer A.
-Looking at the pathway, we notice that if enzyme 3 is inhibited, everything that is
controlled by it will decrease in concentration and activity. That is, the concentration of
D and E will eventually decrease. The activity of enzyme 4 will also decrease, because
it will be acting on a decreased amount of substrate. In addition, if enzyme 3 is inhibited,
more of C will be converted to X through enzyme 5. As such, the concentration of X and
Y is expected to increase, as is the activity of enzyme 6. Anything before enzyme 3
should remain unaffected. Therefore, the concentration of B will remain the same.
An infectious agent is probably a virus instead of a bacterium if it:
a) lacks membrane-bound organelles
b) cannot reproduce in acellular culture
c) has a length of 1?m, about the size of a mitochondrion
d) contains DNA - Answer Answer: B
Viruses possess DNA or RNA but not both, require a host cell's reproductive machinery
in order to reproduce, and have a size 10-100nm. For the MCAT: eukaryotic cell >
bacterium (roughly size of mitochondrion) > virion (roughly size of protein, roughly 100x