Answer: It will DECREASE the rate of reaction
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What will happen if you introduce a competitive inhibitor?
Competitive Inhibition - an overview | ScienceDirect Topics
Effect of different inhibitors on Km and Vmax
Effect of different inhibitors on Km and Vmax
In the presence of a competitive inhibitor higher concentrations of substrate are required to obtain the same rate as in its absence . There is an apparent reduction in affinity of the enzyme for the substrate (increased K m). The reactions in the presence of …
At the macroscopic level the effect of competitive inhibition is to increase the substrate concentration required to achieve a given reaction velocity ; in other words to raise the K m. The V max is unchanged however. Select either uninhibited or inhibited from the boxes below. Then click in the image area to see the course of an uninhibited or a competitively inhibited enzymatic reaction.
Fri Sep 18 2015 · when a competitive inhibitor is present which mimics the substrate and binds with the enzyme but is not converted to any product and competes for the enzyme active site with actual substrate. in simple terms enzymes activity decrease in presence of Competitive inhibitor
What will happen if you introduce a competitive inhibitor ? It will DECREASE the rate of reaction. What will increase the rate of an enzymatic reaction? Add more enzyme add more substrate and adjust pH to optimal level ... Enzyme reactions can be slowed or halted using inhibitors . True.
Fri Sep 14 2018 · Competitive inhibitor does not change the Vmax on an enzyme but increases Km . Uncompetitive inhibitors bind to the site on the enzyme other than the active site. The inhibitor will only bind to the enzyme that is already bound to the substrate and will stop the enzyme from creating product. Uncompetitive inhibitor lowers Vmax and lowers Km. Noncompetitive inhibitor can bind eithe...
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