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What is varied when tested the effect of pH enzyme activity?
The pH is varied to effect, by its affect, this test.
Does the allosteric effect in an enzyme change the enzyme's function?
Yes, the allosteric effect can change an enzyme's function by altering its activity or affinity for its substrate. This modulation is often achieved by a molecule binding to a site on the enzyme other than the active site, causing a conformational change that affects the enzyme's catalytic activity.
What does a kinase enzyme do?
A kinase enzyme adds phosphate groups to proteins, a process called phosphorylation. This modification can change the activity, function, or location of the target protein, which is crucial for many cellular processes such as cell signaling, growth, and differentiation.
How does initial concentration of substrate effect enzyme activity?
At low concentration of substrate , rate of enzyme action is directly proportional to conc. of substrate .
What is the effect of subsrtrate concentration on enzyme activity?
The effect of substrate concentration on enzyme activity is characterized by an initial increase in reaction rate as substrate concentration rises, leading to more frequent enzyme-substrate collisions. However, this relationship reaches a saturation point where all active sites of the enzyme molecules are occupied, resulting in a maximum reaction rate known as Vmax. Beyond this saturation point, further increases in substrate concentration do not enhance enzyme activity, as the enzymes are already working at their maximum capacity. Thus, enzyme activity is dependent on substrate concentration up to a certain threshold, after which it plateaus.
Can hormones alter the enzyme activity in cells?
Yes. Hormones may stimulate the reversible covalent modification of an enzyme via phosphorylation or dephosphorylation and alter the activity of the molecule.
What are Three ways to control enzyme?
One way to control an enzyme is through post-translational modification such as phosphorylation or glycosylation. Other ways to control enzymes are through enzyme induction, inhibition, or by compartmentalizing the metabolic pathways.
What is an autophosphorylation?
An autophosphorylation is the phosphorylation of a kinase protein catalyzed by its own enzymatic activity.
Phosphorylation of glycogen phosphorylase has what effect on the enzyme?
Activation, conversion from glycogen phosphorylase B to glycogen phosphorylase A
What variable did you test in each setup?
We tested the effect of different temperatures on enzyme activity in Setup 1 and the effect of varying pH levels on enzyme activity in Setup 2.
What is varied when testing the effect of pH on enzyme activity?
pH
What is varied when tested the effect of pH enzyme activity?
The pH is varied to effect, by its affect, this test.
What is the effect of hydrochloric acid on the enzyme activity?
Hydrochloric acid can denature enzymes by disrupting their structure and altering their active site. This can impact the enzyme's ability to catalyze chemical reactions effectively, potentially leading to a decrease or loss of enzyme activity.
How does inorganic phosphate inhibit enzyme activity?
Inorganic phosphate can inhibit enzyme activity by competing with the substrate for the enzyme's active site. This can prevent the substrate from binding to the enzyme and undergoing the catalytic reaction. Additionally, inorganic phosphate may alter the enzyme's conformation, affecting its ability to catalyze the reaction.
What enzyme catalyze the phosphorylation of glucose after a meal?
glucokinase
Does the allosteric effect in an enzyme change the enzyme's function?
Yes, the allosteric effect can change an enzyme's function by altering its activity or affinity for its substrate. This modulation is often achieved by a molecule binding to a site on the enzyme other than the active site, causing a conformational change that affects the enzyme's catalytic activity.
What is the effect of cold temperatures on enzyme activity?
Cold temperatures can slow down enzyme activity by decreasing the kinetic energy of molecules, leading to fewer molecular collisions and reduced enzyme-substrate interactions. This can affect the rate of chemical reactions catalyzed by enzymes, as they typically have an optimal temperature range for activity. Ultimately, prolonged exposure to extreme cold temperatures can denature enzymes and render them nonfunctional.
