Thank you for putting this video together! One note, I think the graph at ~7:00 is slightly incorrect and misleading for the non-competitive inhibitor (green line). The way it is shown, the non-competitive inhibitor line does not cross the 1/2Vmax line which means that the Km can't be calculated from that graph (even though you correctly say that they have the same Km). To be correct, I believe the non-competitive line (green line) would follow the uninhibited line (blue line) until after they both cross the 1/2Vmax line at the same place (which would indicate that they have the same Km), and then plateau above the 1/2Vmax line but below the uninhibited Vmax (meaning the NCI has a lower Vmax). That threw me for a loop at first so I just wanted to point it out in case it confused anyone else. Thanks again!
Why do we include uncompetitive inhibition in reversible inhibition if we can't reverse it by increasing substrate concentration? Or is there any other way of reversing uncompetitive inhibition?
How do the non competitive inhibitor never block ES complex formation? I mean if non competitive inhibitor changes the shape of active site that means substrate will not be able to bind to the active site, hence ES complex would not form right? So isn't it blocking the ES complex formation?
Thank you for putting this video together! One note, I think the graph at ~7:00 is slightly incorrect and misleading for the non-competitive inhibitor (green line). The way it is shown, the non-competitive inhibitor line does not cross the 1/2Vmax line which means that the Km can't be calculated from that graph (even though you correctly say that they have the same Km). To be correct, I believe the non-competitive line (green line) would follow the uninhibited line (blue line) until after they both cross the 1/2Vmax line at the same place (which would indicate that they have the same Km), and then plateau above the 1/2Vmax line but below the uninhibited Vmax (meaning the NCI has a lower Vmax). That threw me for a loop at first so I just wanted to point it out in case it confused anyone else. Thanks again!
Great observation, thank you for pointing it out. You are absolutely right that green line should be above 1/2 V max...
Thank you so much
This is the best way to explaining... thank you soooooo much..its help me a loooootttt.....
Cleared here👍
Life saver! Thank you so much for this video sir
Man that was a great video
Well explained
thanks dear ❤️
Thank you this is very helpful
Why do we include uncompetitive inhibition in reversible inhibition if we can't reverse it by increasing substrate concentration? Or is there any other way of reversing uncompetitive inhibition?
How do the non competitive inhibitor never block ES complex formation? I mean if non competitive inhibitor changes the shape of active site that means substrate will not be able to bind to the active site, hence ES complex would not form right? So isn't it blocking the ES complex formation?
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