Back
to top
Feedback inhibition help please
Watch this thread
Announcements
Page 1 of 1
Go to first unread
Skip to page:
anactualmess
Badges:
10
Rep:
?
You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#1
What is the advantage of end-product inhibition being non-competitive rather than competitive?
0
reply
username3249896
Badges:
12
Rep:
?
You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#2
Report
#2
Non-competitive inhibitors will inhibit the enzyme function at any substrate concentration.
The effect of competitive inhibition is reduced at high substrate concentration.
So end-product inhibition being non-competitive means the metabolic process proceeds with greater efficiency. Less wastage of resources as inhibition occurs at all substrate concentrations.
The effect of competitive inhibition is reduced at high substrate concentration.
So end-product inhibition being non-competitive means the metabolic process proceeds with greater efficiency. Less wastage of resources as inhibition occurs at all substrate concentrations.
0
reply
macpatgh-Sheldon
Badges:
20
Rep:
?
You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#3
Report
#3
Hi,
A COMPETITIVE inhibitor of an enzyme, as the name tells you, COMPETES with the substrate for active sites on the enzyme. Therefore, the higher the substrate conc-n, the lesser the efficacy of the inhibitor.
Conversely, a non-competitive inhibitor, also called an irreversible inhibitor (as you cannot reduce its activity by increasing the concentration of substrate, due to its irreversible binding to the active site), is, (to repeat) not competing with the substrate for active sites.
It is easier to understand with an example:-
The antichoninesterase drugs used to treat myasthenia gravis, act by competitively blocking the decomposition of acetylcholine (ACh) by cholinesterase [into acetic acid and choline]; therefore, they can be safely used to treat the disease in which auto-antibodies against the ACh receptor destroy these receptors [in some patients, there are also anti-MUSK antibodies (Abs against MUscle Specific Kinase)], in case of overdose, there is a chance of recovery using drugs that inhibit the action of ACh (on muscarinic and nicotinic receptors).
However, in the case of the organophosphates (used as insecticides), the anticholinesterase action is non-competitive and irreversible, so can be fatal (ideally to insects ONLY!). Some snake venoms have a similar action.
M
A COMPETITIVE inhibitor of an enzyme, as the name tells you, COMPETES with the substrate for active sites on the enzyme. Therefore, the higher the substrate conc-n, the lesser the efficacy of the inhibitor.
Conversely, a non-competitive inhibitor, also called an irreversible inhibitor (as you cannot reduce its activity by increasing the concentration of substrate, due to its irreversible binding to the active site), is, (to repeat) not competing with the substrate for active sites.
It is easier to understand with an example:-
The antichoninesterase drugs used to treat myasthenia gravis, act by competitively blocking the decomposition of acetylcholine (ACh) by cholinesterase [into acetic acid and choline]; therefore, they can be safely used to treat the disease in which auto-antibodies against the ACh receptor destroy these receptors [in some patients, there are also anti-MUSK antibodies (Abs against MUscle Specific Kinase)], in case of overdose, there is a chance of recovery using drugs that inhibit the action of ACh (on muscarinic and nicotinic receptors).
However, in the case of the organophosphates (used as insecticides), the anticholinesterase action is non-competitive and irreversible, so can be fatal (ideally to insects ONLY!). Some snake venoms have a similar action.
M
0
reply
X
Page 1 of 1
Go to first unread
Skip to page:
Quick Reply
