Biochemistry | Enzyme Inhibition
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- čas přidán 25. 04. 2017
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In this lecture Professor Zach Murphy will present on enzyme inhibition. We hope you enjoy this lecture and be sure to support us below!
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Slight correction: for a competitive inhibitor higher km = decreased affinity for substrate
you are essentially saying the same thing....in the last video he talked about how at 1/2vmax [s]=km so the km is basically telling you the concentration of substrate required to reach vmax....he talked about how basically increasing km results in decreased substrate affinity i.e you need to increase [s] to reach vmax
thank you i was just wondering this!!
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I think something is off about the Competitive Inhibitor. If the Substrate Affinity goes up, the KM decreases, but as the Substrate Affinity goes down the KM increases. You explained that to beat the Competitive Inhibitor the Substrate Affinity must go up thus the KM will increase. No, I think the correct explanation is because the Competitive Inhibitor beat the Substrate's Affinity, the Substrate Affinity goes down hence the KM goes up. Because the effect of Competitive Inhibitor is KM goes up but Vmax unaffected. That's all from me, anyway amazing video! Really helps me understand difficult concepts!
Why does the Km decrease of 'uncompetitive inhibition' then? How has the substrate infinity increased?
yes, it's true the rise in Km means that there is a lower substrate affinity for the substrate and enzyme to make ES complex due to low km it takes for inhibitor as well as the high affinity for the inhibitor. So because enzyme has high affinity for the inhibitor it must be fixed. To fix it he has to increase the substrate concentration.
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I agree! but awesome video still...
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Thanq for preking up the learning process😊.I have a doubt :disulfiram used to treat chronic alcoholism is an example of what type of inhibitor?
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At the end of the non competitive inhabitation, how is the inhabitant released and the pocket fixed or removed?
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careful! at 8:56! from what i understand, km has an INVERSE relationship with affinity. what's written on the board looks fine but when you say "km, or affinity, increases" is not!
Km increases , it increases the substrate(S) concentration and decreases the substrate affinity
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good explanation but I've got one question or one thing I don't understand. You said that when the substrate concentration will increase the Km will increase to and so the affinity. In the first part of the video you said that a high Km means that the enzyme has low substrate affinity. So how can the affinity become high in competitive inhibitor when the Km and substrate concentration increases?
This , i am confused as well
Their website is up and running with all these videos and extensive notes on them, so I guess more extensive than the videos are already, I’m going to check it out to seek clarification
I think the idea, some enzymes have low affinity towards substrate so it has to reach high km in order to compete with the inhibitor and make the reaction
Fantastic!
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The fact that aspirin is an irreversible inhibitor is actually why the dosage for aspirin as a bloodthinner is a lot lower than the dosage for aspirin as an anti-inflammatory drug, which I think is super interesting.
Hi is there a video on purine and pyrimidine metabolism?
It makes everything so easy .
Really helpful ,keep going,😊
How can a certain amount of substrate in a cell be specific when there is different amounts of enzymes in a cell at any given moment?
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Thanks sir
Спасибо за мотивацию учить английский
Sir I want notes what you write on board so that I can revise them.
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Great explanation, nice job! But I am a bit confused here..... does this mean that in the presence of an irreversible inhibitor no catalysis will occur? I mean not at all? No matter the amount of substrate there is, non will bind to the enzyme? No effect on Km or Vmax?
Hi dr would you Please post the list of order of the lectures ?