At which point is an enzyme saturated with substrate?
At which point is an enzyme saturated with substrate?
(B) As the concentration of substrate increases, the enzyme becomes saturated with substrate. As soon as the catalytic site is empty, more substrate is available to bind and undergo reaction.
What region of the enzymes does the substrate enter?
the active site
The part of the enzyme where the substrate binds is called the active site (since that’s where the catalytic “action” happens). A substrate enters the active site of the enzyme. This forms the enzyme-substrate complex.
What is the saturation point of an enzyme?
As the substrate concentration increases, the enzyme reaction increases until all of the active sites are occupied by the substrate. When all active sites are occupied, the enzyme is saturated. At this saturation point, adding more substrate makes no difference to the reaction rate.
Which of the following will be true regarding enzyme saturated with substrate?
point Increasing the substrate concentration will appreciably increase the reaction rate Any excess substrate will shift the equilibrium towards the product end of the reaction An enzyme with lower Km is more easily saturated than an enzyme with high Km At saturating levels of substrate, competitive inhibitor will …
What is the difference between active site and catalytic site?
Active site is a region on an enzyme to which the substrates of a chemical reaction bind in order to undergo a catalyzed chemical reaction whereas binding site is a region on a protein, DNA or RNA, to which ligands can bind. This is the key difference between active site and binding site.
How do you know if an enzyme is saturated?
The saturation point is reached when the enzymes are all occupied and are never searching for substrates. The only way to increase the reaction rate once the saturation point is reached is to increase the amount of enzymes.
When an enzyme is saturated it quizlet?
If an enzyme is saturated with substrate, and it is operating at optimum pH and optimum temperature, there is very little that can be done except to increase the enzyme concentration. Some enzymes can be activated further by allosteric activators, in which case one might add some activator to the reaction.
When an enzyme solution is saturated with substrate The most effective way to obtain even faster yield of products would be?
If an enzyme solution is saturated with substrate, the most effective way to obtain an even faster yield of products is to: Add more of the enzyme.
Why do enzyme-catalyzed reactions show saturation?
Saturation of the enzyme means that all of the E is bound to S and no free E exists. The enzyme has bound to as much substrate as possible. This situation occurs at high levels of S.