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An enzyme inhibitor is a substance that reduces or blocks the activity of an enzyme. Enzymes normally speed up chemical reactions in the body or in microorganisms. An inhibitor can prevent a substrate from binding, alter the enzyme's shape, or interfere with another step in the reaction. Many medicines work by inhibiting an enzyme involved in disease or normal physiology.
read more about enzyme inhibitor ...Enzyme inhibitors bind to an enzyme, an enzyme-substrate complex, or another site that controls enzyme activity. This reduces the rate at which the enzyme converts a substrate into a product. The effect can be reversible when the inhibitor can separate from the enzyme or irreversible when it forms a lasting bond or causes permanent inactivation. The strength and duration of inhibition depend on the inhibitor, enzyme, concentration, and surrounding conditions.
Competitive inhibitors interfere with substrate binding, commonly by occupying the active site. Noncompetitive and mixed inhibitors bind at other sites and change enzyme activity in different ways. Uncompetitive inhibitors bind only after the substrate has attached to the enzyme. Irreversible inhibitors permanently disable enzyme molecules until the body produces new ones.
Enzyme inhibitors are used to treat cardiovascular disease, infections, cancer, pain, high cholesterol, diabetes, and many other conditions. Angiotensin-converting enzyme inhibitors reduce production of angiotensin II, while statins inhibit an enzyme involved in cholesterol synthesis. Protease inhibitors can disrupt viral replication, and cyclooxygenase inhibitors reduce prostaglandin production. The clinical effect depends on which enzyme is targeted and where that enzyme functions.
Side effects can result from reducing the intended enzyme activity too much or from affecting related enzymes. Some inhibitors alter liver enzymes that metabolize other medicines, which can raise or lower drug concentrations. The effect can persist after a dose is stopped when inhibition is irreversible or when the inhibitor remains in the body for a long time. Patients should have their medicines, supplements, organ function, and monitoring needs reviewed for the specific inhibitor.
No. Enzyme inhibitors include medicines, natural substances, laboratory chemicals, and toxins. Only selected inhibitors have established therapeutic uses.
A competitive inhibitor and the normal substrate compete for binding in a mutually exclusive way, commonly at the enzyme's active site. Increasing the substrate concentration can reduce the inhibitor's effect under suitable conditions.
No. Some inhibitors bind temporarily, while irreversible inhibitors permanently inactivate the affected enzyme molecules. Recovery from irreversible inhibition usually requires production of new enzyme.
Yes. Inhibiting drug-metabolizing enzymes can increase the concentration and toxicity of another medicine. The interaction depends on the enzyme, inhibitor strength, dose, and other drug.
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