Enzyme Inhibition quiz #1 Flashcards
Enzyme Inhibition quiz #1
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What is enzyme inhibition?
Enzyme inhibition is the process by which compounds called enzyme inhibitors decrease an enzyme's initial reaction velocity (v0), slowing down or stopping the enzyme-catalyzed reaction. What are enzyme inhibitors?
Enzyme inhibitors are specific compounds that interfere with product formation by decreasing the initial reaction rate of enzyme-catalyzed reactions. How do enzyme inhibitors affect the initial reaction velocity (v0) of an enzyme?
Enzyme inhibitors decrease the initial reaction velocity (v0) of an enzyme, slowing down the rate at which the enzyme catalyzes its reaction. With which forms of the enzyme can inhibitors interact?
Inhibitors can interact with either the free enzyme (E) or the enzyme-substrate complex (ES), forming EI or ESI complexes, respectively. What is the EI complex in enzyme inhibition?
The EI complex is formed when an inhibitor binds to the free enzyme (E), preventing substrate binding and decreasing enzyme activity. What is the ESI complex in enzyme inhibition?
The ESI complex is formed when an inhibitor binds to the enzyme-substrate complex (ES), further inhibiting the enzyme's activity. Why do cells use enzyme inhibitors?
Cells use enzyme inhibitors to regulate enzyme activity and as defense mechanisms against pathogens. How can enzyme inhibitors be used as a defense mechanism?
Cells can secrete enzyme inhibitors to act as poisons, inhibiting enzymes in harmful pathogens and protecting the cell. What are the main categories of enzyme inhibitors?
The main categories of enzyme inhibitors are irreversible, reversible, competitive, uncompetitive, mixed, and noncompetitive inhibitors. What is an irreversible inhibitor?
An irreversible inhibitor, also known as an inactivator, binds permanently to an enzyme, inactivating it. What is a reversible inhibitor?
A reversible inhibitor binds non-covalently to an enzyme, and its inhibitory effect can be reversed by removing the inhibitor. What is a competitive inhibitor?
A competitive inhibitor binds to the active site of the free enzyme, competing with the substrate and preventing substrate binding. What is an uncompetitive inhibitor?
An uncompetitive inhibitor binds only to the enzyme-substrate complex (ES), forming an ESI complex and inhibiting enzyme activity. What is a mixed inhibitor?
A mixed inhibitor can bind to both the free enzyme (E) and the enzyme-substrate complex (ES), affecting enzyme activity in multiple ways. What is a noncompetitive inhibitor?
A noncompetitive inhibitor is a type of mixed inhibitor that binds equally well to the free enzyme and the enzyme-substrate complex, reducing enzyme activity regardless of substrate concentration. How do enzyme inhibitors regulate enzyme activity within a cell?
Cells produce enzyme inhibitors to slow down or stop enzyme-catalyzed reactions when enough product has been made, maintaining metabolic balance. How can enzyme inhibitors be used in medicine?
Enzyme inhibitors can be used as drugs to treat diseases by targeting specific enzymes involved in disease processes. What determines whether an inhibitor binds to the free enzyme, the enzyme-substrate complex, or both?
The type of inhibitor determines whether it binds to the free enzyme, the enzyme-substrate complex, or both. What is the effect of enzyme inhibitors on product formation?
Enzyme inhibitors decrease product formation by reducing the enzyme's ability to catalyze reactions. Why might a cell want to decrease an enzyme's initial reaction rate?
A cell may want to decrease an enzyme's initial reaction rate to regulate metabolic pathways and prevent overproduction of products. How do competitive inhibitors affect substrate binding?
Competitive inhibitors compete with the substrate for binding to the enzyme's active site, blocking substrate access. How do uncompetitive inhibitors affect enzyme activity?
Uncompetitive inhibitors bind only to the enzyme-substrate complex, preventing the reaction from proceeding to product formation. How do mixed inhibitors differ from competitive and uncompetitive inhibitors?
Mixed inhibitors can bind to both the free enzyme and the enzyme-substrate complex, whereas competitive inhibitors bind only to the free enzyme and uncompetitive inhibitors bind only to the enzyme-substrate complex. What is the main effect of noncompetitive inhibition on enzyme activity?
Noncompetitive inhibition reduces the maximum reaction velocity (Vmax) of the enzyme without affecting substrate binding affinity (Km). How do irreversible inhibitors inactivate enzymes?
Irreversible inhibitors form covalent bonds with enzymes, permanently inactivating them. What is the role of enzyme inhibitors in protecting cells from pathogens?
Enzyme inhibitors can be secreted by cells to inhibit essential enzymes in pathogens, acting as a defense mechanism. How can enzyme inhibitors be used to control harmful bacteria?
Cells can release enzyme inhibitors into the environment to inhibit bacterial enzymes, slowing or stopping bacterial growth. What is the abbreviation commonly used for enzyme inhibitors?
The letter 'I' is commonly used to abbreviate enzyme inhibitors. What is the abbreviation for the free enzyme?
The free enzyme is commonly abbreviated as 'E.' What is the abbreviation for the enzyme-substrate complex?
The enzyme-substrate complex is abbreviated as 'ES.' What is the abbreviation for the enzyme-inhibitor complex?
The enzyme-inhibitor complex is abbreviated as 'EI.' What is the abbreviation for the enzyme-substrate-inhibitor complex?
The enzyme-substrate-inhibitor complex is abbreviated as 'ESI.' How do enzyme inhibitors contribute to metabolic regulation?
Enzyme inhibitors help regulate metabolic pathways by controlling the activity of enzymes, ensuring proper levels of metabolic products. What is the significance of reversible inhibition in cellular processes?
Reversible inhibition allows cells to temporarily regulate enzyme activity, enabling dynamic control of metabolic pathways. How do cells recognize when to produce enzyme inhibitors?
Cells monitor product levels and produce enzyme inhibitors when enough product has accumulated to prevent overproduction. What is the difference between an EI complex and an ESI complex?
An EI complex forms when an inhibitor binds to the free enzyme, while an ESI complex forms when an inhibitor binds to the enzyme-substrate complex. How can enzyme inhibitors be used as drugs?
Enzyme inhibitors can be designed as drugs to target specific enzymes involved in diseases, thereby treating or managing medical conditions. What is the general effect of all enzyme inhibitors on enzyme-catalyzed reactions?
All enzyme inhibitors decrease the initial reaction velocity (v0) of enzyme-catalyzed reactions. Why is it important for cells to regulate enzyme activity?
Regulating enzyme activity is important to maintain metabolic balance, prevent wasteful overproduction, and respond to environmental changes.
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