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Allosteric enzymes are most effective when the substrate concentration is?
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∙ 15y ago
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Wiki User
∙ 15y ago
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Does Allosteric regulation depends on inhibitors binding to the active site of enzymes?
Of course. That is the meaning of ' noncompetitive inhibitor. ' It does not compete with the substrate at the active site but inhibits enzyme activity at the allosteric ( other site ) site.
What are four things that can affect the way enzymes work?
pH, temperature, concentration of enzyme, substrate concentration, etc
How do enzymes affect reactions?
The initial velocity of a gradually increases during enzyme substrate reaction. The concentration of the substrate also increases with it.
What are 3 characteristics of enzymes?
Temperature/pH/Substrate Concentrate and Inhibitors
Some factors that may influence enzyme activity?
A low temperature can slow down enzyme activity and high temperatures can denature an enzyme making it unusable. pH levels also affect enzyme activity. Every cell has an ideal temperature and pH
How does substrate concentration and pH affect enzymes?
Substrate concentration will affect enzymes because substrates are specific to enzymes. The pH will affect enzymes because certain enzymes will work better in certain pH levels.
What causes the enzymes active site to change shape?
When too much of a certain compound is made, the compound attaches to a separate site called allosteric site. When attached to the allosteric site, it changes the active site's shape and prevents any more to be made.
Why will increasing the substrate concentration not decrease the effect of a non competitive inhibitor?
Because you will still have the same number of enzymes inhibited. For example, you have 20 enzymes and 10 non-competitive inhibitors. Regardless of substrate concentration, at any one time, there will only be 10 enzymes available to accept a substrate. Increasing the substrate concentration does not affect this.
What effect enzymes activity?
Temperature, pH, substrate concentration
Does Allosteric regulation depends on inhibitors binding to the active site of enzymes?
Of course. That is the meaning of ' noncompetitive inhibitor. ' It does not compete with the substrate at the active site but inhibits enzyme activity at the allosteric ( other site ) site.
What happens during allosteric inhibition?
Allosteric (noncompetitive) inhibition results from a change in the shape of the active site when an inhibitor binds to an allosteric site. When this occurs the substrate cannot bind to its active site due to the fact that the active site has changed shape and the substrate no longer fits. Allosteric activation results when the binding of an activator molecule to an allosteric site causes a change in the active site that makes it capable of binding substrate.
How allosteric enzymes differ non allosteric?
Allosteric enzymes have the ability to change their conformational ensemble after binding. This changes their affinity at a different ligand binding site.
What factors affect the rate of reactions of enzymes?
mainly mainly there 41)pH2) temperature3) concentration of enzyme4)concentration of substrate
How are enzymes affected by concentration levels?
Higher concentration will mean that there is a higher probability that the substrate will find the enzyme. There will be a point though that you will start seeing dimishing returns as the concentration is sufficient for every enzyme molecule to have a substrate all the time.
What happens if the enzyme concentration is low?
An enzyme can overcome the presence of a competitive inhibitor by increasing the substrate concentration The reaction rate falls direct propartional to the concentration fall (which is the result of that same reaction). This is called 'first order reaction rate'.
What are four things that can affect the way enzymes work?
pH, temperature, concentration of enzyme, substrate concentration, etc
How do enzymes affect reactions?
The initial velocity of a gradually increases during enzyme substrate reaction. The concentration of the substrate also increases with it.
