They are competitive inhibition, non-competitive inhibition, uncompetitive inhibition, and mixed inhibition are the 4 types of enzyme inhibition.
- competitive inhibition: The enzyme's active site is occupied by a molecule other than the substrate, which results in competitive inhibition. The substrate and the inhibitor (molecule) are structurally and chemically related (hence able to bind to the active site). The competitive inhibitor blocks the active site to prevent substrate binding.
- In non-competitive inhibition, a substance binds to a site different from the active site (an allosteric site). The enzyme's active site changes structurally when the inhibitor binds to the allosteric site. This modification alters the affinity between the active site and substrate, prohibiting substrate binding. In non-competitive inhibition, the inhibitor only binds to the substrate-enzyme complex.
- Uncompetitive inhibition is frequent in reactions involving two or more substrates or products.
- Mixed inhibition: When an inhibitor binds both the enzyme by itself and the enzyme-substrate complex, mixed inhibition occurs. According to this scenario, the inhibitor may bind the enzyme by itself 60% of the time and the enzyme-substrate complex 40% of the time.
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