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because the competitive inhibitor stops the regular substrate from joining the enzyme. Its takes its place in the enzyme.

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Q: Why would the reaction of a normal rate of an enzyme slow down and its substrate slow down when a competitive inhibitor is present?
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Related questions

Is Vmax a threshold of substrate concentration for initiation of an enzymatic reaction?

Oddly phased question in my opinion. Vmax is only effected by the amount of enzyme present in the reaction. Substrate concentration has zero effect on Vmax. There for I believe the answer in no. {Enzyme concentration is responsible for this}


Are substrate and catalyse the same thing?

No! A substrate is a reagent in a chemical reaction. Catalyse is the verb form of catalyst; a catalyst is a chemical species that participates in lowering the energy barrier of a chemical reaction and allow a reaction to occur more rapidly. A catalyst is not consumed in a reaction and therefore only a small amount of catalyst is required in any reaction (if required at all), whereas a substrate must be present in the proper stoichiometric amount to allow a reaction to proceed as it is consumed.


Does the amount or reactant in the cell influence the action of enzymes?

yes, it does. if there is more substrate present, the net reaction will go to the right. but if more prdouct accumulates, the reaction will slow down and eventually begin to move to the left


Why was there no increase in reaction with 8g compared to 4g of substrate?

Generally, if you increase a reagent and there is no increase in the reaction, then it is limited by the amount of another reagent present. For example, a mole of Sodium Hydrogen Carbonate will react with a mole of Acetic Acid. However, doubling the Acetic acid will not result in a greater reaction because it is limited by the amount of Sodium Hydrogen Carbonate present.


What does a strong IKI result indicate?

Substrate is present


What are all of the factors that affect enzyme activity except for temperature and pH?

There are a number of factors that can influence how efficiently a certain enzyme can catalyse a reaction: the amount of substrate present, whether there are chemicals present that inhibit enzymes by either binding to their active site or cofactor site, the amount of enzymes present...


Substrate molecules bind to enzymes where?

The bind in the active site.


What reduces the activity of an enzyme?

In vitro, Temperature, pH and other factors leading to degradation or suboptimal activity affect enzymatic activity. All enzymes are not created equal, each enzyme functions its best at different optimal conditions.


What should be done in order to keep the rate constant over the entire time course?

add more substrate. The rate of the reaction drops when the enzyme no longer has a maximum number of substrate molecules to interact with. Above the maximum substrate concentration, the rate will not be increased by adding more substrate; the enzyme is already working as fast as it can. An enzyme can catalyze a certain number of reactions per second, and if there is not sufficient substrate present for it to work at its maximum velocity, the rate will decrease. Therefore, to keep the enzyme working at its maximum, you must add more substrate.


What substrate is present in the arctic tundra?

Your question makes absolutely no sense.


Enzymes that are produced only when substrate is present are termed?

induced enzyme


Describe the change in the rate of reaction when the enzyme concentration is increased?

The increase of enzyme concentration increase the rate of reaction. Given a fixed amount of substrates, it means that the substrates will be digested faster as there are more enzymes to do the work. Substrate concentration, temperature, and pH value of the surrounding where the enzymes work on also affects the rate.