Bio a level help - end product inhibition
I don't understand the answer, can someone explain it to me?
QS = End-product inhibition is likely to be competitive rather
than non-competitive. Suggest reasons for this, and give
an example of end-product inhibition.
ANSWER = End-product inhibition regulates rate of reaction
(1): concentrations of substrate and product
determine reaction rate (1); (so must be)
competitive (1): substrate concentration has no
effect in non-competitive inhibition (1); e.g. ATP
and PFK in respiration (1).
QS = End-product inhibition is likely to be competitive rather
than non-competitive. Suggest reasons for this, and give
an example of end-product inhibition.
ANSWER = End-product inhibition regulates rate of reaction
(1): concentrations of substrate and product
determine reaction rate (1); (so must be)
competitive (1): substrate concentration has no
effect in non-competitive inhibition (1); e.g. ATP
and PFK in respiration (1).
(edited 2 years ago)
Reply 1
13
The key thing here is, if my Biology memory serves me well, is that competitive inhibition is where the inhibitor competes with the substrate by attaching to the enzyme via the active site.
So this would regulate the rate of reaction for whatever the context is, as enzyme activity is proportional to the rate of reaction. If some enzymes are "blocked" with the inhibitor, this lessens the rate of reaction.
Non-competitive inhibitors instead bind to the allosteric site of an enzyme, which often, denatures the enzyme and consequently usually destroys it. So in a non-competitive inhibitor, the concentration of the substrate has no effect because the active sites of the enzyme become warped - so no amount of substrate can bind to the active site.
So this would regulate the rate of reaction for whatever the context is, as enzyme activity is proportional to the rate of reaction. If some enzymes are "blocked" with the inhibitor, this lessens the rate of reaction.
Non-competitive inhibitors instead bind to the allosteric site of an enzyme, which often, denatures the enzyme and consequently usually destroys it. So in a non-competitive inhibitor, the concentration of the substrate has no effect because the active sites of the enzyme become warped - so no amount of substrate can bind to the active site.
Reply 2
Original post
by dbhc2411The key thing here is, if my Biology memory serves me well, is that competitive inhibition is where the inhibitor competes with the substrate by attaching to the enzyme via the active site.
So this would regulate the rate of reaction for whatever the context is, as enzyme activity is proportional to the rate of reaction. If some enzymes are "blocked" with the inhibitor, this lessens the rate of reaction.
Non-competitive inhibitors instead bind to the allosteric site of an enzyme, which often, denatures the enzyme and consequently usually destroys it. So in a non-competitive inhibitor, the concentration of the substrate has no effect because the active sites of the enzyme become warped - so no amount of substrate can bind to the active site.
So this would regulate the rate of reaction for whatever the context is, as enzyme activity is proportional to the rate of reaction. If some enzymes are "blocked" with the inhibitor, this lessens the rate of reaction.
Non-competitive inhibitors instead bind to the allosteric site of an enzyme, which often, denatures the enzyme and consequently usually destroys it. So in a non-competitive inhibitor, the concentration of the substrate has no effect because the active sites of the enzyme become warped - so no amount of substrate can bind to the active site.
Ahh, i understand, thankss
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