@@dorothyotogbolu6485 lmao im an internet stranger who is studying biochem rn-and was wondering if you had become a doctor after seeing ur comment since u said ur studying MCAT which would mean if u did aight and didnt flop ur gpa prop in med school/gl to ya if ur not tho
That moment when you roam all websites and youtube channels to understand a specified information and literally none talk about it... then you find AK LECTURES simplifying your every doubt and question... seriously.. I'm really amazed. Thank you so much!
Andrey, you deserve a Nobel Peace Prize for your contribution to the knowledge of mankind ! You are very gifted a teacher ! When I graduate from med school, you might not be awarded yet but you will receive my donation!
you are a great man .. your explain is amazingly better than my professor 👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻thank you very much .. you save my life🤣🤣🤣🤣🤣🤣🤣
Hello, would you please help to understand the steady stand conditions where S0 is higher then this mentionned on the curve of Michaelis (initial substrate concentration is small)
What is the problem with using regular rate law to explain the catalysis reaction? Can't we use experiments to determine the order of the reaction? Is it because enzymes are not considered reactants but their concentration actually changes the rate of reaction?
The mathematics makes complete sense but I'm a little confused with how you can assume a steady-state condition. To elaborate: this equation is derived assuming a very specific condition where K1 = K-1+K2. Of course, this is not the case everywhere. For example, if [S] >> [ES] >>>> [E]+[P], then, in my mind, it seems as though it's impossible for K1 = K-1+K2. In these initial conditions, for K1 to equal K-1+K2, you'd have to assume that the catalytic activity of the enzyme corresponds to the binding affinity of the substrate. This is not the case (is it?). Then using an equation we derived in these steady-state conditions, we somehow extrapolate the chemical behavior of these enzymes under other conditions! Like, how can we just assume that we can model enzymatic behavior at Vmax when the conditions are completely different in a situation where we can even begin to talk about Vmax? Any response is appreciated. I feel like I'm missing something fundamental here.
when you explained on the Km constant, you said its units are concentration but isnt that mathematically incorrect because the units cancel out?? at 15 mins.
I have a question regarding steady state, how can enzyme-substrate complex remain constant if it increases throughout the graph? Thank you for your videos.
only the rate of reaction and the concentration of substrate increases throughout the graph. For the enzyme-substrate complex, its like work shifts in this certain analogy. You send someone to work at a place for an hour, then, when one hour has passed, that person leaves the place and you send someone else to go work at that place since that place is free, someone can take the spot to work. Two people can't work at that same place, but at the same time, if the place is empty then fill the job if you can. That way the number of people who work at that place stay constant (the concentration of people at that place stays constant), since only one person can be there at any time. If one person leaves, one enters, and the cycle goes forever...
rate of enzyme = rate of rxn ... only if the reaction cannot occur without the enzyme. (otherwise there will be a basal reaction rate, and enzyme increases the rate of the reaction, and hence "enzyme rate" is a difference of those two). So, we're basically assuming that reaction doesn't occur without the catalysts. Am I understanding that right?
+MimicIsaac i think the answer to that question is, E+S is a new reaction entirely, and you can calculate enzyme rate by just studying that reaction ... without considering what happens when S -> products by itself.
