Decreasing Vmax in uncompetitive inhibition also decreases?
Correct answer: A. Km
- A. Km
- B. Ko
- C. Vo
- D. Both A and B
Explanation
Uncompetitive inhibition occurs when the inhibitor binds to the enzyme-substrate complex (ES) to form an ESI complex, which can no longer convert the substrate to the product. Uncompetitive inhibition does not affect the binding of the substrate to the enzyme, but it decreases the Vmax by decreasing the concentration of available enzyme. Since the Km value is a measure of the enzyme's affinity for the substrate, it is not affected by changes in Vmax due to uncompetitive inhibition. Therefore, decreasing Vmax in uncompetitive inhibition does not affect Ko or Vo, but it does decrease Km.
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Enzymes are biological catalysts that lower activation energy without being consumed, and their specificity is explained by the lock and key and induced fit models. Work includes the effects of temperature, pH and substrate concentration on reaction rate, plus competitive and non-competitive inhibition and how these differ.
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