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Dr, can u explain again about the high km is low affinity in terms of the the concentration of E and S/ concentration of ES?

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Hi, Dr. may I know how to differentiate active site and
docking site ?

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Good evening Dr. Is docking site the site in which the subunits of an enzyme form bonds? Or is it the site at which multiple enzymes form bonds?

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Good Day Dr, I dont quite get what does the statements below mean..

Dear all,
1. For determining Ki, I advise you to the the LB plot (1/v vs 1/[S]), and determine the -1/Km for that particular [I]., becos the -1/Km for that [I] is equal to -1/Km (1 + [I]/Ki), where the Km is the value without the inhibitor

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hello Dr, i have a question regarding the plots. The basic equation used for all the plots are Vmax [S] / Km + [S] then the values are substituted according to the graph. Isnt this the basic MM equation ? Does that mean all graphs follow the basic MM equation but just changes the y, x axis, gradient and c intercept according to their plot ?

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Hello Dr, since we are plotting ECB plot will not be perfect to get only 1 interception point , so if we got many interception points, even there are only 2 lines are intercepted we will count them in? and find average ?

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Salam sejahtera Dr, we have discuss that industry will tend to select enzyme with high Km and high K3 rite. Hence, my question is if the affinity of enzyme towards the substrate is low, will it affect the rate of formation of product? I have thought about one assumption here. If the Km is low and K3 is low, substrate forms into complex very fast and turns slow when getting into product. At the same way, if Km is high and K3 is high, substrate forms into complex slower and turns fast into product. In fact, there still need to wait for the substrate to form into complex before getting into products so no matter how high is the K3 it will be restricted by the high Km (low affinity). That's what i confused with and hope that Dr can solve my problem tq.

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Assalamualaikum Dr. Waalaikumussalam. May I know how can we get v equals to v0 over k3?Sorry, there are no equation as such, v = v/k3. And from where did we get v equals to k3 times [ES]? From the rate of reaction formula, i.e. we measure enzyme activity at [ES] -> [E] + [P]; where this is = k3.This is under the Enzyme Conservation Theory equation. Sorry, no. Enzyme Conversation Eq is [E]t = [E] + [ES]. Thank you Dr.You're welcome :)

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Salam Dr, saya nak tanya tentang Tutorial 2. Adakah unit macam mikro(u) atau milli(m) perlu di ambil kira kalau nak buat graph dan untuk calculation? sebab last answer of any parameter mesti mandatory letak unit. So i was a bit confused if we need to change it or not. If not why?
And lagi satu dr, kita calculate k3 from Vmax and e right. and unit for k3 is sec-1. I wonder macam mana kita dapat sec-1 since unit for Vmax is mol/sec and unit for e is M. And M is mol/L. Macam mana dia potong potong?

Thank youuu Dr :)

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Assalamualaikum Dr. Can you explain more about [S] >>> [E] ? what is the meaning when you said the amount of the substrate  (excess) is no different with the amount of added substrate ? Why ?

thank you Dr.

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Assalamualaikum Dr. I tried answered one question on the internet the characteristics of high catalytic efficiency of enzyme. It turns out the answer for it was low Km and high Kcat. Doesn't it when we have low Km the enzyme is less efficient due to the tight binding?

Thank you Dr.

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Good day Dr. I want to ask for ECB plot, is it a good method to plot Km at negative part of horizontal axis, and Vmax on the vertical axis as per photo for the second question in the Tutorial?

Or only the normal plotting method taught in class only is applicable for ECB plot (plot Km at negative part of horizontal axis, plot Vmax on corresponding positive Km, draw straight line connecting both)?

Thank you Dr :)

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Assalam Dr, i want to ask what is different between dissociation constant in assumption in steady state and dissociation constant of ES complex? And why Km is dissociation constant of ES complex? Not to Km is Michaelis constant?

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Hi Dr, I want to ask, before we plot the graph, the unit of v is (umol sec-1) while the [S] is mM. Do I need to change the unit of v to mmol sec-1?

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A158516

DR , i still confuse how to use this graph and didnt understand the equation

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Excuse me Dr, I still don't really understand the graph for Energy Diagram for enzyme. Dr. said before the lower the graph, the more stable the enzyme-substrate complex. But I thought more negative free energy will be more spontaneous?

2. What means by local dielectric constant lower (means electric insulator?) How does it effect enzyme bind to the active site?

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Dear all,
1. For determining Ki, I advise you to the the LB plot (1/v vs 1/[S]), and determine the -1/Km for that particular [I]., becos the -1/Km for that [I] is equal to -1/Km (1 + [I]/Ki), where the Km is the value without the inhibitor

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Good evening Dr. I want to ask for the tutorial question, is it ok if i draw the graph for only question no. 2 by using excel?