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Example Questions
Example Question #241 : Organic Chemistry, Biochemistry, And Metabolism
Duchenne Muscular Dystrophy is an X-linked recessive genetic disorder, resulting in the loss of the dystrophin protein. In healthy muscle, dystrophin localizes to the sarcolemma and helps anchor the muscle fiber to the basal lamina. The loss of this protein results in progressive muscle weakness, and eventually death.
In the muscle fibers, the effects of the disease can be exacerbated by auto-immune interference. Weakness of the sarcolemma leads to damage and tears in the membrane. The body’s immune system recognizes the damage and attempts to repair it; however, since the damage exists as a chronic condition, leukocytes begin to present the damaged protein fragments as antigens, stimulating a targeted attack on the damaged parts of the muscle fiber. The attack causes inflammation, fibrosis, and necrosis, further weakening the muscle.
Studies have shown that despite the severe pathology of the muscle fibers, the innervation of the muscle is unaffected.
Which of the following would best describe the dystrophin protein?
Signaling protein
Chemical receptor
Transmembrane protein
Ion channel
Fibrous protein
Transmembrane protein
The passage tells us that "dystrophin localizes to the sarcolemma," so we know it is located at the membrane of the muscle fiber. We also know that its role is to structurally link the muscle fiber and the basal lamina. We can eliminate the choices for ion channel, signaling protein, and chemical receptor based on what we know about dystrophin's function. We are left with either fibrous protein or transmembrane protein. Though fibrous proteins also have structural roles, transmembrane protein is the best choice because we know that dystrophin is linking the muscle fiber to another structure, meaning that it must span the membrane.
Example Question #22 : Enzymes And Enzyme Inhibition
Which of the following is FALSE concerning enzymes?
Enzymes increase the amount of product created in a reaction
Substrates must bind the enzyme's active site in order to initiate its effects
Enzymes reduce reaction activation energy
Enzymes are not destroyed in a reaction and can be used in the same reaction countless times
Enzymes increase both the forward rate and reverse rate of a reaction
Enzymes increase the amount of product created in a reaction
Enzymes will increase the rate of a chemical reaction, but will not alter the equilibrium of a reaction. As a result, the amount of product is not affected by enzymes. The same amount of product will be made; it will just be made at a faster rate.
Example Question #21 : Enzymes And Enzyme Inhibition
The end product of an enzymatic reaction inhibits formation of product in an earlier step. This type of enzymatic regulation is known as __________.
enzyme-substrate complex
feedback inhibition
negative regulation
allosteric regulation
metabolic pathway loop
feedback inhibition
Feedback inhibition is a type of regulation in which an enzyme product blocks an earlier part of a metabolic reaction. This allows cells to regulate resources by signaling when enough product is made.
Example Question #31 : Enzymes And Enzyme Inhibition
A pathway of reversible enzymatic reactions is given below. Enzymes are denoted by letters, and products by numbers.
If the enzyme C is blocked by an allosteric inhibitor, what will happen to each of the products?
Concentrations of product 1, 2, and 3 will decrease; concentrations of product 4 and 5 will increase
Concentration of product 5 will decrease; concentrations of product 3, 2, and 1 will increase
Concentration of product 4 will decrease; concentration of product 3 will increase
Concentrations of product 4 and 5 will decrease; concentration of product 3 will increase
Concentrations of product 4 and 5 will decrease; concentrations of product 1, 2, and 3 will increase
Concentrations of product 4 and 5 will decrease; concentrations of product 1, 2, and 3 will increase
All upstream products, prior to the action of enzyme C, will start to increase in concentration because each enzyme is reversible. Directly, product 3 will build up and product 4 will decrease. This will lead product 5 to decrease because there is no 4 to make it. As 3 builds up, enzyme B will start working in reverse, converting it back into product 2, according to Le Chatelier's principle. Then, when 2 starts to build up, it will also be converted backwards into product 1.
Example Question #32 : Enzymes And Enzyme Inhibition
Among the most important pH buffer systems in humans is the bicarbonate buffer, which keeps the blood at a remarkably precise 7.42 pH. The bicarbonate buffer system uses a series of important compounds and enzymes to make the system function. Figure 1 depicts the key reactions that take place.
The activity of this buffer system is mainly controlled by the renal and respiratory systems. The renal system excretes bicarbonate in the urine, while the respiratory system “blows off” carbon dioxide as needed. By balancing these two systems as needed, blood pH is maintained in such a narrow range.
A protein is discovered that inhibits carbonic anhydrase activity. It does so by reversibly binding to the active site typically occupied by carbonic acid and thus preventing carbonic acid from binding. This would most likely be what kind of inhibitor?
Noncompetitive
Competitive
Conformational
Uncompetitive
Allosteric
Competitive
Reversible binding in the active site is typical of a competitive inhibitor. Other kinds of inhibitors bind to the active site after the normal substrate has already bound, such as in uncompetitive inhibition. Alternatively, allosteric inhibitors can bind to sites other than the active site and induce a shape change that diminishes affinity for the typical substrate.
Example Question #31 : Enzymes And Enzyme Inhibition
A student is conducting an experiment in which he adds an inhibitor to an enzyme-catalyzed reaction. When the student first adds the inhibitor, the reaction rate decreases, however, he can return the reaction rate to normal by adding a large quantity of substrate. What type of inhibitor is the student using?
A competitive inhibitor
A substrate-sensitive inhibitor
A noncompetitive inhibitor
An uncompetitive inhibitor
The student likely made a mistake—this result could not occur regardless of the type of inhibition
A competitive inhibitor
Only competitive inhibition can be overcome by the addition of more substrate. Competitive inhibitors work by binding to and blocking the enzyme's active site. If more substrate is added, it increases the chance that an enzyme molecule will bind to the substrate instead of the inhibitor. Noncompetitive inhibition is not affected by the amount of substrate, uncompetitive inhibition is not tested on the MCAT, and "substrate-sensitive" is not a type of inhibition.
Example Question #34 : Enzymes And Enzyme Inhibition
Which statement is true about noncompetitive inhibitors?
They alter the conformation of the enzyme.
They bind at the active site of the enzyme.
They bind covalently to the enzyme and disrupt the substrate from attaching.
They actively block the enzyme from attaching to the substrate.
They alter the conformation of the enzyme.
Noncompetitive inhibitors do not bind at the active site of an enzyme. Instead, they bind at another position on the enzyme and alter its conformation. This passive approach to inhibition makes an enzyme unable to attach to the substrate at the active site. Only irreversible inhibitors bond covalently; both competitive and noncompetitive inhibitors bind noncovalently.
Example Question #32 : Enzymes And Enzyme Inhibition
Diisopropylflourophosphate (DFP) is an example of an enzyme inhibitor. It covalently binds to a serine residue in the active site of a serine protease, thus inactivating the enzyme.
Based on this information, what type of enzyme inhibitor is DFP?
Noncompetitive inhibitor
Proenzyme
Irreversible inhibitor
Competitive inhibitor
Irreversible inhibitor
Whenever you read that an enzyme inhibitor has covalently bonded to an enzyme, you can conclude that it is an irreversible inhibitor. Both competitive and noncompetitive inhibitors bind noncovalently to the target enzyme.
Example Question #32 : Enzymes And Enzyme Inhibition
Which of the following is not an example of positive feedback?
As blood calcium levels increase, parathyroid hormone (PTH) is reduced.
A forest fire slowly expands outward, which provides it with even more fuel to burn.
During childbirth, oxytocin creates a stimulus which causes the hypothalamus to release more oxytocin.
As more buffalo begin to run in a herd, the overall level of panic increases. This results in even more buffalo running.
As blood calcium levels increase, parathyroid hormone (PTH) is reduced.
Negative feedback provides the body with a method for shutting down a reaction once sufficient product has been created. Parathyroid hormone (PTH) is responsible for increasing blood calcium levels, but once the level is sufficient, the parathyroid glands detect the sufficient calcium level and no longer produce PTH. PTH works in coordination with calcitonin to maintain this balance via its negative feedback loop.
Positive feedback, in contrast, involves the exponential increase of a reaction upon detection. Very few examples of positive feedback exist in the body, though oxytocin follows this model during childbirth.
Example Question #81 : Macromolecules
Sulfanilamide is an antibiotic that resembles the intermediate, 4-aminobenzoic acid (PABA), in the metabolic pathway to create folic acid. It binds to the active site of the enzyme that normally binds to PABA, and inhibits the binding of PABA temporarily. Since folic acid is necessary for bacterial growth, this antibiotic helps inhibit the spread of infection in humans.
Based on this information, what type of inhibitor is sulfanilamide?
Uncompetitive inhibitor
Irreversible inhibitor
Competitive inhibitor
Noncompetitive inhibitor
Competitive inhibitor
Competitive inhibitors block substrates by binding noncovalently to the active site on enzymes. This prevents the substrate from entering the active site.
Noncompetitive inhibitors, in contrast, will act on regions outside of the active site to prevent binding. Uncompetitive inhibition is a specialized form of noncomptitive inhibition in which the inhibitor binds to the enzyme complex after the substrate has entered the active site. Irreversible inhibitors form covalent bonds, and fall outside the common inhibitor classifications.
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