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Understanding Competitive and Non-Competitive Enzyme Inhibition: Kinetics and Mechanisms

This article delves into the concepts of enzyme kinetics, specifically focusing on competitive and non-competitive inhibition. It discusses the structural interactions between substrates, enzymes, and inhibitors, providing clarity on terms such as Kmapp and Vmax. The mechanisms governing these types of inhibition are explored, showing how inhibitors influence enzymatic activity and the rates of reactions. Practical implications in biochemistry and pharmacology are also considered, highlighting the relevance of understanding enzyme behavior in drug design and metabolic regulation.

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Understanding Competitive and Non-Competitive Enzyme Inhibition: Kinetics and Mechanisms

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Presentation Transcript

  1. EI S E S + E ES E + P + I 0 0 0 0 Kmapp/Vmax Kmapp -1/Kmapp Inhibicja kompetycyjna CI 0 0 CI – inhibitor kompetycyjny; S – substrat; E – enzym; No I – brak inhibitora

  2. Inhibicja niekompetycyjna S EI ESI NCI S E S + E ES E + P + + I I 0 0 0 0 1/Vmaxapp Km/Vmaxapp 0.5Vmax 0 0 NCI – inhibitor niekompetycyjny; S – substrat; E – enzym; No I – brak inhibitora

  3. EI S + E ES E + P + I Inhibicjaakompetycyjna UCI S E 0 0 0 0 1/Vmaxapp 0.5Vmax Kmapp/Vmaxapp Kmapp 0 0 -1/Kmapp UCI – inhibitor akompetycyjny; S – substrat; E – enzym; No I – brak inhibitora

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