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An enzyme's activity can appear to exceed 100% due to a cascade effect where the enzyme catalyzes multiple cycles of a reaction, leading to a cumulative amplification of the reaction. However, it is important to note that enzyme activity is typically expressed as a rate, which is a measure of the amount of substrate converted per unit time, and therefore cannot be greater than 100%.
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What is the effect of phosphorylation on enzyme activity?
Phosphorylation of an enzyme can either activate or inhibit its activity, depending on the specific enzyme and the site of phosphorylation. Addition of a phosphate group can change the shape or conformation of the enzyme, affecting its ability to bind substrates or cofactors. These changes can lead to either an increase or decrease in enzymatic activity.
Will enzyme activity increase with an increase in temperature?
Warmer temperatures mean little more than that molecules are moving more rapidly. This promotes enzyme activity on its own, however, as movement allows the enzymes to react to more material in a shorter amount of time.
What would be the likely outcome if you increased the concentration of substrate for an enzyme in the presence of a noncompetitive inhibitor?
Increasing the concentration of substrate will not overcome the effect of a noncompetitive inhibitor. The inhibitor binds to the enzyme at a site other than the active site, causing a conformational change that reduces the enzyme's activity. Therefore, increasing the concentration of substrate will not result in a significant increase in enzyme activity.
If an enzyme has been inhibited noncompetitively?
If an enzyme has been inhibited noncompetitively, the inhibitor binds to the enzyme at a site other than the active site, altering the enzyme's shape and reducing its activity. This type of inhibition is not overcome by increasing the substrate concentration.
Chemical mechanisms that can turn off or reduce an enzyme are what?
Inhibitors can turn off or reduce enzyme activity by binding to the enzyme and blocking its active site, preventing substrates from binding. Competitive inhibitors compete with substrates for the active site, while non-competitive inhibitors bind to a different site on the enzyme, altering its shape and reducing its activity. allosteric inhibitors bind to a site on the enzyme other than the active site, causing a conformational change that reduces enzyme activity.
How does a noncompetitive enzyme inhibitor function to inhibit enzyme activity?
A noncompetitive enzyme inhibitor works by binding to the enzyme at a site other than the active site, causing a change in the enzyme's shape. This change makes it harder for the substrate to bind to the enzyme, reducing its activity.
What conclusion can be drawn about the action of the enzymes as the temperature increase?
enzyme A becomes less effective earlier than enzyme B enzyme b stays effective at higher temperatures than enzyme a
What is the effect of phosphorylation on enzyme activity?
Phosphorylation of an enzyme can either activate or inhibit its activity, depending on the specific enzyme and the site of phosphorylation. Addition of a phosphate group can change the shape or conformation of the enzyme, affecting its ability to bind substrates or cofactors. These changes can lead to either an increase or decrease in enzymatic activity.
Some enzymatic regulation is allosteric In such cases which of the following would usually be found?
In allosteric enzyme regulation, the regulator molecule binds to a site other than the active site, called the allosteric site. This binding alters the enzyme's activity by inducing a conformational change in the enzyme structure. This can either activate or inhibit the enzyme's function, depending on the nature of the allosteric regulator.
Will enzyme activity increase with an increase in temperature?
Warmer temperatures mean little more than that molecules are moving more rapidly. This promotes enzyme activity on its own, however, as movement allows the enzymes to react to more material in a shorter amount of time.
Is the enzyme activity same at 5 and 25 Centigrade temperature in water?
The specific activity of an enzyme at a specific temperature will be dependent on both the temperature the enzyme is operating at as well as the concentrations of the substrates (the starting materials of the reaction that the enzyme catalyzes) and products (the end materials of the reaction) present around the enzyme. However, as a general rule, the activity of an enzyme will be different at at 5 centigrade than it will be at 25 centigrade.
An enzyme whose activity is affected when a molecule binds to a certain site other than the active site is called?
an allosteric enzyme
The graph below shows how two different enzymes react with a substrate as the temperature increases. Based on the results what conclusion can be drawn about the action of the enzymes as?
Based on the graph, it can be concluded that one enzyme is more temperature-sensitive than the other. This is evident by the steeper slope of one enzyme's curve, indicating a faster increase in activity with temperature. Additionally, both enzymes exhibit an optimum temperature where their activity is highest before declining due to denaturation.
What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?
Allosteric inhibitors bind to a specific site on an enzyme (allosteric site) other than the active site, inducing a conformational change that decreases enzyme activity. This alteration prevents the substrate from binding to the active site, thus blocking the enzyme's ability to catalyze reactions.
What would be the likely outcome if you increased the concentration of substrate for an enzyme in the presence of a noncompetitive inhibitor?
Increasing the concentration of substrate will not overcome the effect of a noncompetitive inhibitor. The inhibitor binds to the enzyme at a site other than the active site, causing a conformational change that reduces the enzyme's activity. Therefore, increasing the concentration of substrate will not result in a significant increase in enzyme activity.
How does allosteric inhibition differ from noncompetitive inhibition in terms of their mechanisms of action on enzyme activity?
Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Noncompetitive inhibition, on the other hand, involves a molecule binding to the enzyme at a site other than the active site, but it does not change the enzyme's shape. This type of inhibition reduces the enzyme's activity by blocking the active site or altering the enzyme's ability to bind to the substrate.
In a survey 365 girls and 345 boys were asked What is your favorite sport If 7.4 percent of the girls and 10.1 percent of the boys chose biking how many more boys than girls chose this activity?
There were about 34 boys, and about 27 girls, so about 7 more boys than girls choose this activity.
