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What else can I help you with?
Why does a reaction slow down the time?
Usually:decreasing concentrationlowering the temperaturesometimes lowering pressureremoving any catalyst
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 happens to the radioactive isotopes that are released in a nuclear reaction?
they decay over 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'.
How do inhibitors regulate enzymes?
Competitive inhibition: Where an inhibitor, which has a similar molecular shape to the enzyme's substrate, competes with substrate to fit to the enzymes active site. In the end all substrate can be broken down because the competitive inhibitors are not permanently bonded to the enzymes active site. If there is a higher concentration of substrate the amount of time it will take for all the substrate to be broken down will be less than if there is a higher concentration of inhibitor. Non-competitive inhibition: Where the inhibitor attaches itself to the enzyme at a site which is NOT the active site. This causes the enzymes shape to be changed slightly which would mean that the substrate is unable to fit to the active site. Non-competitive inhibitors do no compete with the substrate for the active site, hence their name. Non-competitive inhibitors may be permanent or not. Because the inhibitor and substrate are not competing for the same site an incrase in substrate concentration does not decrease the inhibitors effect.
If you have an enzymatic reaction proceeding at the optimum pH and optimum temperature You add a competitive inhibitor to the reaction and notice that the reaction slows down?
Exactly. If a reaction is going as fast as it can go (optimum) and you add an inhibitor (something to impede it) it slows down. This could be done to prevent excessive heat or too much gas at one time.
Why does a reaction slow down the time?
Usually:decreasing concentrationlowering the temperaturesometimes lowering pressureremoving any catalyst
What does a competitive inhibitor bind to?
A competitive inhibitor is a molecule that binds to the active site of an enzyme, to prevent substrates entering the active site and therefore lowering the rate of reaction. Some drugs act as competitive inhibitors to control reactions in the body, and the body also releases competitive inhibitors as a means of self control. But remember that the amount of product formed is still remain the same, only the time taken increased.
What happens to your reaction time when hands are warm?
you get warm
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 happens to the radioactive isotopes that are released in a nuclear reaction?
they decay over time
What happens to your reaction time when you get older?
When you get older, your reaction time becomes naturally slower this is because your body is not at it's fittest peak compared to what it would of been in your youth.
What is reaction time in sport?
If you are in a race and your reaction time is slow, when you hear the starting gun-shot, you won't start on time therefore not winning.
What happens when a reaction is at equilibrium?
When a reaction is at equilibrium, the rate of the forward reaction is equal to the rate of the reverse reaction. This means that the concentrations of reactants and products remain constant over time, creating a balanced state where no further changes occur.
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'.
How do inhibitors regulate enzymes?
Competitive inhibition: Where an inhibitor, which has a similar molecular shape to the enzyme's substrate, competes with substrate to fit to the enzymes active site. In the end all substrate can be broken down because the competitive inhibitors are not permanently bonded to the enzymes active site. If there is a higher concentration of substrate the amount of time it will take for all the substrate to be broken down will be less than if there is a higher concentration of inhibitor. Non-competitive inhibition: Where the inhibitor attaches itself to the enzyme at a site which is NOT the active site. This causes the enzymes shape to be changed slightly which would mean that the substrate is unable to fit to the active site. Non-competitive inhibitors do no compete with the substrate for the active site, hence their name. Non-competitive inhibitors may be permanent or not. Because the inhibitor and substrate are not competing for the same site an incrase in substrate concentration does not decrease the inhibitors effect.
What blocks enzyme activity by binding to the active site of an enzyme?
Competitive inhibitors reduce enzyme activity by binding (in competition with the enzyme's substrate) to the active site. These inhibitors may be reversible or irreversible. With reversible inhibitors, which may release the enzyme, concentrations much higher than the concentration of the substrate would be required to completely block enzyme activity, and even then one or two reactions may take place over long periods of time. With irreversible inhibitors, which permanently attach to the enzyme, enzyme activity could be completely blocked when the amount of inhibitor matches the amount of enzyme. Competitive inhibition reduces the enzymes ability to bind substrate (so it lowers the KM) but does not alter the maximum rate (very high substrate concentrations would out compete for enzyme binding).Other types of inhibitors work in other ways. Non-competitive inhibitors bind to the enzyme on a site other than the active site. These too may be reversible or irreversible. Binding does not compete with substrate, so concentrations to completely block enzyme activity do not have to be as high as reversible competitive inhibitors. Non-competitive inhibition reduces the apparent maximum rate for the enzyme.Uncompetitive inhibitors bind only when the substrate is also bound to the enzyme (they bind to the enzyme-substrate complex). Both the maximum rate and substrate binding affinities appear lower.
