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The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis- Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect on the maximal velocity, Vmax, and Michaelis constant, KM , of the hypothetical enzyme. Experimental condition Vmax Км Twice as much enzyme is used. No change Doubles Half as much enzyme is used. Half as large Half as large A competitive inhibitor is present. Doubles Decreases An uncompetitive inhibitor is present. Increases Increases A pure noncompetitive inhibitor is present. Decreases No change

The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis- Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect on the maximal velocity, Vmax, and Michaelis constant, KM , of the hypothetical enzyme. Experimental condition Vmax Км Twice as much enzyme is used. No change Doubles Half as much enzyme is used. Half as large Half as large A competitive inhibitor is present. Doubles Decreases An uncompetitive inhibitor is present. Increases Increases A pure noncompetitive inhibitor is present. Decreases No change

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme.

For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.

 

The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis-Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect on the maximal velocity, \( V_{\text{max}} \), and Michaelis constant, \( K_M \), of the hypothetical enzyme. | Experimental condition | \( V_{\text{max}} \) | \( K_M \) | |-------------------------------------------------|----------------------|---------------| | Twice as much enzyme is used. | Doubles | No change | | Half as much enzyme is used. | Half as large | No change | | A competitive inhibitor is present. | No change | Increases | | An uncompetitive inhibitor is present. | Decreases | Decreases | | A pure noncompetitive inhibitor is present. | Decreases | No change |
Transcribed Image Text:The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis-Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect on the maximal velocity, \( V_{\text{max}} \), and Michaelis constant, \( K_M \), of the hypothetical enzyme. | Experimental condition | \( V_{\text{max}} \) | \( K_M \) | |-------------------------------------------------|----------------------|---------------| | Twice as much enzyme is used. | Doubles | No change | | Half as much enzyme is used. | Half as large | No change | | A competitive inhibitor is present. | No change | Increases | | An uncompetitive inhibitor is present. | Decreases | Decreases | | A pure noncompetitive inhibitor is present. | Decreases | No change |
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