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.
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!
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.
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.
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?
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?
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.?
+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.
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.
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The best biochemistry videos on youtube, perfect for university level biochem! Thank you!
I honestly don't know how i would have passed many of my exams if not for your teachings. We really appreciate everything you do! Thank You.
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.
I will probably pass pharmacology this semester because of these videos
I’m taking a 16 week Biochemistry course in 4 weeks and your videos have been super helpful. Thank you for that!
I would much rather pay you than these professors. You can explain something in 15 minutes that takes my professor an hour. You are a life saver!
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!
LOVE your videos! Have been watching them throughout the years and your explanations help me understand complicated topics. Thank you!!
Incredibly amazing explanation. Thank you very much.
You make me appreciate science much more! Very clear and intellectual way of connecting the dots! Thanks!!
I really don’t know what to do if this channel didn’t exist .
Perfect AK lectures and very very easy for everyone even those in pre-school.
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.
how fortunate to attend your class I wish I could do it GOAT keep it up I honestly like this ak lecture channel
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.
Thank so much sir!. with respect to all teachers out there, you're the best there is. THANK YOU!!!!
You're so good in explaining.
Wel explained...👍👍
Thk u sir for your consultation about enzyme inhibition . It helps me to clear my doubt
thank you you are the best doing these explanations , before seeing your videos i was so confused
you are amazing , please please keep going
Inbitors go to the enzyme bind to it shape the shape and stop production or the original functional of that enzyme
OMG I hate my biochem textbook. Thank you for helping me out on my uni-level biochem XD
Perfect! Thx for this well explained video!
smartest guy on TH-cam
Thank you so much! This was such a tremendous help. Excellent explanation.
it really helped thank you proffesor andrey .... perfect explination
thank you thank you!!!
Ak always brings something you can relate to, you're a star!!! Ak😉
very clearly explained everything, thank you so much
thanks for the video
it was very useful to me and my friends
It resembles the enzyme pattern however it's only similar not perfect so it causes that enzyme to not function
I think homeboy is great👍🏼👌🏻👊🏽
Thanks sir 🥰 clearly understood
Hats off to you.
more than amazing thank you very much
excellent review!
Ur lectures r very good
You are so good at explaining these topics. Thank you.
Thanks man! Very helpful stuff...
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fucking love this guy
Thank you so much !
what is the difference between poisons and inhibitors?
I actually understand
Penicillin helps production
I wish i found these videos sooner :/
thank you lots!
Thsnk yuo ...very much....🌺🌺🌺🌺
I don't always drink.... but when I do.... I prefer XX...
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?
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?
Thank you🌸🌸🌸
Thank you so so soooooooooooooooo much
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thank you
Starts at 8:20
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What that means is
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is it true if i say the substrate affinity for the enzyme's active site is higher than the inhibitor's in uncompetitive inhibition?
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.?
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
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...
Mirin
Man I miss your accent
Indian voices hurt my ears
You talk too much!
How do u think he's supposed to make people understand without talking
then read a book duh
Ak always brings something you can relate to, you're a star!!! Ak😉
plz explain kcat/km graphically in relation to different enzymes for same substrate
Best explanation I'm get knowledge which can help to answer different questions
Thank you very much sir for to solve my problems.
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.
textbook answer lol
by non covalent did u mean even ionic bonds please help @AK LECTURES
3 ESI looking sus
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You have the best videos! Thank you so much and keep going!
Hi sir, can u tell me, is molybdate competative inhibitor or non competative?
These are so good, thank u so much!
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