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Exploring reversible enzyme inhibition, this overview discusses competitive, uncompetitive, and non-competitive inhibitors and their effects on enzyme kinetics. It delves into the quantification of enzyme-inhibitor affinity through dissociation constants (Ki and Ki'), and the use of graphical methods like Lineweaver-Burk plots for interpreting inhibition data. The text also highlights the importance of reversible inhibitors in the design of drugs, with examples such as DHFR and HIV protease inhibitors.
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Competitive inhibitors compete with the substrate for the active site of the enzyme, reducing its activity
Uncompetitive inhibitors bind exclusively to the enzyme-substrate complex, reducing enzyme activity
Non-competitive inhibitors can bind to either the enzyme alone or the enzyme-substrate complex, reducing enzyme activity
Inhibitors can alter the Km value, which reflects the affinity of the enzyme for its substrate
Inhibitors can alter the Vmax value, which reflects the maximum rate of the enzyme-catalyzed reaction
The Ki value quantifies the affinity between an enzyme and its inhibitor
The Ki' value quantifies the affinity of a non-competitive inhibitor for the enzyme-substrate complex
The Lineweaver-Burk plot is a graphical method used to visualize the effects of reversible enzyme inhibitors on enzyme kinetics
Nonlinear regression is a more precise method for determining kinetic parameters and inhibitor effects
Partially competitive inhibition occurs when an inhibitor binds to the enzyme-substrate complex without completely blocking enzyme activity
Substrate or product inhibition occurs when a substrate or product molecule acts as an inhibitor, affecting enzyme activity
Slow-tight inhibition involves a time-dependent change in the enzyme-inhibitor complex, resulting in enhanced inhibition over time
Multi-substrate analogue inhibitors are designed to target enzymes with multiple substrates, creating a single, highly selective and potent inhibitor molecule
Reversible enzyme inhibitors can be designed to structurally resemble the natural substrates of their target enzymes
Transition state analogs take advantage of the enzyme's preference for the transition state, resulting in higher binding affinity
Inhibitors can be designed with stability and resistance to enzymatic degradation in mind for effective pharmaceutical development
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Definition of Enzyme Inhibitors
Molecules that decrease enzyme activity by binding to the enzyme.
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Impact of Reversible Inhibitors on Km and Vmax
Competitive: Increases Km, no change in Vmax. Uncompetitive: Decreases Km and Vmax. Non-competitive: No change in Km, decreases Vmax.
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Characteristics of Reversible Inhibition
Inhibitor binds transiently, reducing activity without permanent enzyme damage.
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