GOB Chemistry
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Consider the three forms of enzyme inhibition (competitive, uncompetitive, and irreversible). Determine if the statement below is true or false. If false, correct the statement:
Each of the three kinds of inhibition involves the formation of covalent bonds with the enzyme.
Classify the inhibition described below as uncompetitive, competitive, or irreversible: A certain drug is used to manage a specific viral infection. The drug works by binding to the enzyme in the virus and does not dissociate.
Determine the kind of inhibition (uncompetitive, competitive, or irreversible) present in the following:
A certain pesticide works by attaching itself to an allosteric site on an insect’s digestive enzymes and slowing down their activity without permanently inactivating them.
A reversible type of enzyme inhibition of mercury can be stopped by chelation therapy using DMSA. Describe this type of mercury inhibition.
Identify the type of product that could potentially serve as a competitive inhibitor for the enzyme that facilitates its production.
True or False: A competitive inhibitor can be identified from an uncompetitive inhibitor by increasing the substrate concentration and monitoring the reaction's rate change.
Which type of enzyme inhibitor is often considered poison? Explain your answer.
How does the rate of a biochemical reaction catalyzed by an enzyme change when the concentration of a non-competitive inhibitor is increased, keeping the substrate concentration constant?
How does the rate of a biochemical reaction catalyzed by an enzyme change when the concentration of a non-competitive inhibitor is decreased, keeping the substrate concentration constant?
Identify the type of enzyme regulation in the scenario below:
The conversion of phosphoenolpyruvate to pyruvate, catalyzed by pyruvate kinase, is inhibited by high concentrations of alanine. Note that in this reaction, alanine is neither a product nor a substrate.
Determine whether the following scenario describes a competitive or a noncompetitive enzyme inhibitor:
A researcher discovers that a new drug binds directly to the active site of a key metabolic enzyme, preventing the natural substrate from binding.
Determine the type of inhibition the following scenario describes:
In an enzyme-catalyzed reaction, an inhibitor that does not resemble the substrate in structure is added and it decreases the reaction rate.
During a biochemical experiment, it was found that α-ketoglutarate acts as an inhibitor of isocitrate dehydrogenase.
Would α-ketoglutarate act as a competitive or noncompetitive inhibitor?
The drug ciprofloxacin targets a specific type of enzyme in treating human bacterial infections. Which of the following best describes the action of ciprofloxacin?
The enzyme xanthine oxidase is responsible for converting hypoxanthine to xanthine, and xanthine to uric acid. High levels of uric acid in the body cause gout. The substance allopurinol inhibits xanthine oxidase and is used to treat gout. Does allopurinol compete with hypoxanthine and xanthine for the active site of xanthine oxidase, or does it bind to a different site on the enzyme?
In the treatment of hypertension, a patient is prescribed captopril, a medication known to affect the renin-angiotensin system. Is captopril considered a reversible or irreversible inhibitor of angiotensin-converting enzyme (ACE)?
Methanol (CH3OH) is a toxic substance that can lead to blindness or death if ingested. It is metabolized in the liver by the same enzyme that metabolizes ethanol. The toxic metabolites of methanol are formaldehyde (HCHO) and formic acid (HCOOH). The administration of an intravenous ethanol solution is used as a treatment for methanol poisoning. How could this method help in preventing the toxic effects of methanol ingestion?