Give some examples for competitive inhibition?
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In competitive inhibition, an inhibitor that resembles the normal substrate binds to the enzyme, usually at the active site, and prevents the substrate from binding. ... For example, methotrexate is a chemotherapy drug that acts as a competitive inhibit
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Competitive inhibition is interruption of a chemical pathway owing to one chemical substance inhibiting the effect of another by competing with it for binding or bonding. Any metabolic or chemical messenger system can potentially be affected by this principle, but several classes of competitive inhibition are especially important in biochemistry and medicine, including the competitive form of enzyme inhibition, the competitive form of receptor antagonism, the competitive form of antimetabolite activity, and the competitive form of poisoning (which can include any of the aforementioned types). This article examines the enzymatic class.
In competitive inhibition of enzyme catalysis, binding of an inhibitor prevents binding of the target molecule of the enzyme, also known as the substrate.[1] This is accomplished by blocking the binding site of the substrate – the active site – by some means. The Vmax indicates the maximum velocity of the reaction, while the Km is the amount of substrate needed to reach half of the Vmax. Km also plays a part in indicating the tendency of the substrate to bind the enzyme.[2]Competitive inhibition can be overcome by adding more substrate to the reaction, which increases the chances of the enzyme and substrate binding. As a result, competitive inhibition alters only the Km, leaving the Vmax the same.[3] This can be demonstrated using enzyme kinetics plots such as the Michaelis-Menten or the Lineweaver-Burk plot. Once the inhibitor is bound to the enzyme, the slope will be affected, as the Km either increases or decreases from the original Km of the reaction.[4][5][6]
Most competitive inhibitors function by binding reversibly to the active site of the enzyme.[1] As a result, many sources state that this is the defining feature of competitive inhibitors.[7] This, however, is a misleading oversimplification, as there are many possible mechanisms by which an enzyme may bind either the inhibitor or the substrate but never both at the same time.[1] For example, allosteric inhibitors may display competitive, non-competitive, or uncompetitive inhibition.[1]
In competitive inhibition of enzyme catalysis, binding of an inhibitor prevents binding of the target molecule of the enzyme, also known as the substrate.[1] This is accomplished by blocking the binding site of the substrate – the active site – by some means. The Vmax indicates the maximum velocity of the reaction, while the Km is the amount of substrate needed to reach half of the Vmax. Km also plays a part in indicating the tendency of the substrate to bind the enzyme.[2]Competitive inhibition can be overcome by adding more substrate to the reaction, which increases the chances of the enzyme and substrate binding. As a result, competitive inhibition alters only the Km, leaving the Vmax the same.[3] This can be demonstrated using enzyme kinetics plots such as the Michaelis-Menten or the Lineweaver-Burk plot. Once the inhibitor is bound to the enzyme, the slope will be affected, as the Km either increases or decreases from the original Km of the reaction.[4][5][6]
Most competitive inhibitors function by binding reversibly to the active site of the enzyme.[1] As a result, many sources state that this is the defining feature of competitive inhibitors.[7] This, however, is a misleading oversimplification, as there are many possible mechanisms by which an enzyme may bind either the inhibitor or the substrate but never both at the same time.[1] For example, allosteric inhibitors may display competitive, non-competitive, or uncompetitive inhibition.[1]
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