if a medical student understands anything and everything related to chemical eqautions and maths ...that means something has been greatly taught.............well done sirrrr..........

You are by far one of my favorite lecturers I have ever come across. You are incredibly thorough. You do not waste any time on unrelated material nor do you have unnecessary pauses and you are fast without losing me ever. I never want to jump ahead to get to the point because I know I will miss something important that will make me see the material in a new and helpful way.

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So, the reason Km decreases for uncompetitive is because the substrate does not release, thus having high affinity, and the Km stays the same on the noncompetitive because the substrate does release?

What's the difference between the graphs(Lineweaver) of Noncompetitive and Mixed inhibition? How can I differentiate mixed from the others?

I got it about changing Km in uncompetitive and not competative inhibition. Bouth makes not functional ESI but in not competitive ESI can convert in ES but in uncompetitive it can't(Km it's concentration of S when ES it's half saturated). So when we need half saturated ES we will get in non competative inhibition because I(inhibitor) can be let in ESI but uncompetitive inhibition I(inhibitor) can't be let of ESI so there we will have some not functional ES because they stay in ESI form.

i woof you♥

You said that the substrate is able to bind to the enzyme's active site regardless if there is a non-competitive inhibitor is present, but doesn't the presence of the inhibitor change the active site in a way that the substrate is no longer able to bind?

seriously why not fit this in part 1???

Why is km unchanged in non competitive inhibiton- i think the explanation is wrong.

Explanation is good but please take some breath in between or pause so that it will give some time to us to better understand the things..

why do you have these extra 1 minute videos