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This is the most thorough and complete video about enzyme inhibition that I have seen so far. Excellent video. One nitpicky question/concern that I have. I have also I heard of a scenario where the inhibitor binds allosterically and then changes the enzyme conformation so that the substrate does not bind. The Khan Academy video talks about that scenario and he said that it works out to be similar to competitive inhibition in practice because either the substrate is bound or the inhibitor is bound but never both (if I remember right). He calls this scenario allosteric competitive inhibition, though I don't know if anyone else refers to it that way. I checked out the wikipedia article about Mixed Inhibition and it seems that this scenario is a type of mixed inhibition. Article talks about situation where inhibitor binds allosterically and decreases apparent affinity of the enzyme for substrate, says this situation mimics competitive inhibition. So I guess it would have helped me if he talked about mixed inhibtion a bit more. In any case still a fantastic video, thanks so much for everything you do AK Lectures.
Importantly, for competitive inhibition, the inhibitor likely has a higher affinity for the active site because the active site is shaped like the transition-state intermediate of the reaction. Many competitive inhibitors are shaped like this intermediate because the active site has a much higher affinity for the intermediate structure compared to the substrate structure.
Many biological systems that utilize enzymes must be able to regulate their activity. One means of enzyme regulation involves using special agents called inhibitors (molecules or sometimes ions) that bind onto the enzymes and inhibit their activity. There are two categories of inhibitors - irreversible inhibitors and reversible inhibitors. In irreversible inhibition, the inhibitor binds very tightly to the enzyme either via covalent or non-covalent means and ultimately does not dissociate very easily, if at all, from the enzyme. Some examples of irreversible inhibitors include nerve gas, penicillin and aspirin. In reversible inhibition, the inhibitor binds onto the enzyme but can dissociate relatively easily under the proper conditions. There are four major subdivisions of reversible inhibition - competitive inhibition, uncompetitive inhibition, non-competitive inhibition and mixed inhibition. In competitive inhibition, the inhibitor resembles the substrate and binds directly to the active site. Increasing the concentration of the substrate can overcome the competitive inhibitor. In uncompetitive inhibition, the substrate must bind onto the active site before the inhibitor can bind onto the enzyme. This is because the binding of the substrate onto the enzyme creates an allosteric site on that enzyme that was not previously there. The inhibitor can now bind onto that allosteric site and create the enzyme-substrate-inhibitor complex. This complex will not go on to produce the product. Increasing the substrate concentration will not overcome an uncompetitive inhibitor. In non-competitive inhibition, the enzyme has a permanent allosteric site that the inhibitor can bind to. In addition, the inhibitor can bind to the allosteric site regardless of whether or not the substrate is bound to the active site. Increasing the substrate concentration will not effect the non-competitive inhibitor. Mixed inhibition is a more complex form of reversible inhibition in which the binding of the inhibitor essentially decreasing the affinity of the active site for the substrate and decreases the ability of the substrate to produce product molecules.
For the uncompetitive inhibitor, I thought that enzymes can only undergo a conformational change when a ligand binds to its allosteric site? But you said that the substrate has to bind to its active site to make a conformational change? Was my information incorrect?
Sir, is it possible in competitive inhibition that 50%substrate and 50% inhibitor binds with active site of enzyme at the same time reducing the concentration of product.?
excellent explanation- however why is uncompetitive inhibition a sub tyoe of reversible inhibition if the inhibition cannot be overcome by increasing the conc of the substrate, wouldnt that mean its irreversible
The difference is in the binding. For the irreversible once the e+ I is made it no longer can dissociate. For uncompetitive the inhibitor can leave the allosteric set making the enzyme usable once more. Does that help?
+ali wassim it depends, some are irreversible others reversible. Cyanide is reversible non-competitive. it binds to ferric ion of cytochrome oxidase, but it binds better to the ferric ion of methemoglobin, which has low levels in the body. administering sodium nitrate causes extra methemoglobin production. causing cyanide to form cyanomethemoglobine.
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Absolutely wonderful; I have been working on understanding these issues for about two months and in just one hour of watching these lectures things are finally becoming clear. Job well done!
You just save my life!!!! I’m studying for my medicine test, Step 1. You are the best teacher ever. God bless you so much!!!!!! Gracias desde el fondo de mi ♥️. I love your accent by the way.
This is the most thorough and complete video about enzyme inhibition that I have seen so far. Excellent video. One nitpicky question/concern that I have. I have also I heard of a scenario where the inhibitor binds allosterically and then changes the enzyme conformation so that the substrate does not bind. The Khan Academy video talks about that scenario and he said that it works out to be similar to competitive inhibition in practice because either the substrate is bound or the inhibitor is bound but never both (if I remember right). He calls this scenario allosteric competitive inhibition, though I don't know if anyone else refers to it that way. I checked out the wikipedia article about Mixed Inhibition and it seems that this scenario is a type of mixed inhibition. Article talks about situation where inhibitor binds allosterically and decreases apparent affinity of the enzyme for substrate, says this situation mimics competitive inhibition. So I guess it would have helped me if he talked about mixed inhibtion a bit more. In any case still a fantastic video, thanks so much for everything you do AK Lectures.
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Thk u sir for your consultation about enzyme inhibition . It helps me to clear my doubt
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Importantly, for competitive inhibition, the inhibitor likely has a higher affinity for the active site because the active site is shaped like the transition-state intermediate of the reaction. Many competitive inhibitors are shaped like this intermediate because the active site has a much higher affinity for the intermediate structure compared to the substrate structure.
Thank you very much sir for to solve my problems.
Many biological systems that utilize enzymes must be able to regulate their activity. One means of enzyme regulation involves using special agents called inhibitors (molecules or sometimes ions) that bind onto the enzymes and inhibit their activity. There are two categories of inhibitors - irreversible inhibitors and reversible inhibitors. In irreversible inhibition, the inhibitor binds very tightly to the enzyme either via covalent or non-covalent means and ultimately does not dissociate very easily, if at all, from the enzyme. Some examples of irreversible inhibitors include nerve gas, penicillin and aspirin. In reversible inhibition, the inhibitor binds onto the enzyme but can dissociate relatively easily under the proper conditions. There are four major subdivisions of reversible inhibition - competitive inhibition, uncompetitive inhibition, non-competitive inhibition and mixed inhibition. In competitive inhibition, the inhibitor resembles the substrate and binds directly to the active site. Increasing the concentration of the substrate can overcome the competitive inhibitor. In uncompetitive inhibition, the substrate must bind onto the active site before the inhibitor can bind onto the enzyme. This is because the binding of the substrate onto the enzyme creates an allosteric site on that enzyme that was not previously there. The inhibitor can now bind onto that allosteric site and create the enzyme-substrate-inhibitor complex. This complex will not go on to produce the product. Increasing the substrate concentration will not overcome an uncompetitive inhibitor. In non-competitive inhibition, the enzyme has a permanent allosteric site that the inhibitor can bind to. In addition, the inhibitor can bind to the allosteric site regardless of whether or not the substrate is bound to the active site. Increasing the substrate concentration will not effect the non-competitive inhibitor. Mixed inhibition is a more complex form of reversible inhibition in which the binding of the inhibitor essentially decreasing the affinity of the active site for the substrate and decreases the ability of the substrate to produce product molecules.
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plz explain kcat/km graphically in relation to different enzymes for same substrate
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Inbitors go to the enzyme bind to it shape the shape and stop production or the original functional of that enzyme
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For the uncompetitive inhibitor, I thought that enzymes can only undergo a conformational change when a ligand binds to its allosteric site? But you said that the substrate has to bind to its active site to make a conformational change? Was my information incorrect?
is it true if i say the substrate affinity for the enzyme's active site is higher than the inhibitor's in uncompetitive inhibition?
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It resembles the enzyme pattern however it's only similar not perfect so it causes that enzyme to not function
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Hi sir, can u tell me, is molybdate competative inhibitor or non competative?
Sir, is it possible in competitive inhibition that 50%substrate and 50% inhibitor binds with active site of enzyme at the same time reducing the concentration of product.?
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by non covalent did u mean even ionic bonds please help @AK LECTURES
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excellent explanation-
however why is uncompetitive inhibition a sub tyoe of reversible inhibition if the inhibition cannot be overcome by increasing the conc of the substrate, wouldnt that mean its irreversible
The difference is in the binding. For the irreversible once the e+ I is made it no longer can dissociate. For uncompetitive the inhibitor can leave the allosteric set making the enzyme usable once more. Does that help?
what is the difference between poisons and inhibitors?
Penicillin helps production
Wow
Am kinda confused pls, is allosteric inhibition the same as uncompetitive inhibition?
Allosteric inhibition is binding to the allosteric site, whilst uncompetitive inhibition involves binding to the enzyme-substrate complex
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How we can stop a non competitive inhibitor ??? i need it pleaaaase answer
+ali wassim it depends, some are irreversible others reversible. Cyanide is reversible non-competitive. it binds to ferric ion of cytochrome oxidase, but it binds better to the ferric ion of methemoglobin, which has low levels in the body. administering sodium nitrate causes extra methemoglobin production. causing cyanide to form cyanomethemoglobine.
+Mitchel Dijkhof Thanx , most of non competitive are reversible , so i need more details of how we can stop them. Please help me i need that answer...
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