Enzyme Kinetics- is my summary correct?

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In summary, this conversation is about the kinetics of enzyme reactions. Part 1 is dependent on the Km value, Part 2 is dependent on the Kcat value, and the entire enzyme reaction is dependent on the ratio of Kcat to Km (or Kcat/Km). If the Km value is higher than the Kcat value, then Part 1 will happen quickly and produce product. If the Km value is lower than the Kcat value, then Part 1 will happen slowly and produce product. If the Km and Kcat values are the same, then Part 1 will happen at a constant rate and produce product.
  • #1
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I have been looking at this enzyme kinetics stuff forever and was trying to come up with a summary for things... #=_=

Is this even right...? :/

|---------------|This segment I'm calling "Part 2"
k1 k2
E + S
equilibrium.png
ES
rarrow.png
E + P
k-1
|---------------|This segment I'm calling "Part 1"

Part 1 and Part 2 are separate reactions, but together, they form the overall enzyme reaction.
Part 1 is dependent on the Km value, Part 2 is dependent on the Kcat value, and the entire enzyme reaction is dependent on the ratio of Kcat to Km (or Kcat/Km).

Part 1:
Since it is dependent on the Km value, and Km = (k-1 + k2)/k1, which means
(ES breakdown)/(ES formation), you have to ask, "Is the ES breakdown higher than the formation?"
If yes, then it means
spinup.png
Km, so ES tends to break down (slow).
If no,
spindown.png
Km, so ES tends to stay together (fast rxn).

Part 2:
Have to ask, "Is Kcat high or low?"
If high, fast product formation.
If low, slow product formation.So for the entire enzyme-catalyzed reaction, it seems like there would only be these 4 possibilities:

1.
spinup.png
Kcat +
spinup.png
Km = slow for ES to form, but once it does, quickly generates product.2.
spinup.png
Kcat +
spindown.png
Km = fast for ES to form and quickly generates product.3.
spindown.png
Kcat +
spinup.png
Km = slow for ES to form, and once it does, slowly generates product.4.
spindown.png
Kcat +
spindown.png
Km = fast for ES to form, but slowly generates product.
...Well, is any of this even right?
sad.gif

Please help me! D:
Thank you SO much!
smiley.gif
 
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  • #2
What book are you using?

The general derivation of Michaelis-Menton kinetics is based upon the steady-state approximation.

In the case of modeling Enzyme kinetics, it says that the change in concentration of the Enzyme-Substrate complex [ES] with time is zero.

The speed with which ES forms is given by k1[E]. The rate of destruction of ES is given by -k-1[ES] - k2[ES] (falling back or going to products)

Km is more like an equilibrium constant. Think about the case without any reaction (k2 very small). If this is the case, then k1[E] = k-1[ES] (definition of equilibrium)
Keq = [ES]/[E] = k1/k-1 (looks almost like 1/Km)

I think the usual way of thinking abou this is similar to the way you described above, except you think about things in terms of how much enzyme is tied up with substrate and the speed with which the enzyme reacts once it has boud substrate.
 
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  • #3
I find your statements tending to the 'not even wrong' I'm afraid.

Formation of ES being fast or slow is irrelevant because in the assumptions of steady-state you are treating a situation where all that is going to be formed already has been. So that leaves the questions how much has been formed? how fast does it give product?

At saturation ( [Substrate] >> Km) practically all the enzyme is in the form ES. The rate is simply kcatEtotal.
The higher kcat the faster the reaction.

Instead if substrate concentration is low such that S << Km your can see your equation simplifies so that v is still proportional to kcat but then also to 1/Km

The first is simple and as before, the second is because the higher the Km the less ES complex there is (at low S!) to be catalysed.
At every stage you should look at formulas but also consider the physical situations they represent, go between one and the other at every
stage.

I am sorry about these unintended cancellations, an artefact of the system. :(
 
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  • #4
Looks like we cannot write S in square brackets! :oldgrumpy:
 
  • #5
epenguin said:
Looks like we cannot write S in square brackets! :oldgrumpy:
So that's what is causing all of the strikethroughs?
 
  • #6
I think so. We should use x for S and then EX for the complex I guess.
 
  • #7
Add a space [ S].
 
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  • #8
Borek said:
Add a space [ S].

Yes thank you, I had worked out to try that which I would have done if there had been any more comeback on this thread, :oldsmile:.
 

1. What is Enzyme Kinetics and why is it important?

Enzyme kinetics is the study of the rate at which enzymes catalyze chemical reactions. This is important because enzymes play a crucial role in many biological processes and understanding their kinetics can help us better understand and manipulate these processes.

2. How do enzymes affect reaction rates?

Enzymes increase the rate of a reaction by lowering the activation energy required for the reaction to occur. This allows the reaction to happen more quickly and efficiently.

3. What factors can affect enzyme activity?

The activity of enzymes can be influenced by various factors such as temperature, pH, substrate concentration, and the presence of inhibitors or activators. Changes in these factors can alter the rate of enzyme-catalyzed reactions.

4. What is the Michaelis-Menten equation and what does it represent?

The Michaelis-Menten equation is a mathematical model that describes the relationship between the substrate concentration and the reaction rate of an enzyme. It represents the maximal reaction rate (Vmax) and the substrate concentration at which the reaction rate is half of Vmax (Km).

5. How can enzyme kinetics be applied in research and industries?

Enzyme kinetics is widely used in research to study enzymes and their mechanisms, and to develop new drugs and treatments. In industries, enzyme kinetics is utilized in the production of various products such as food, pharmaceuticals, and biofuels, as enzymes can increase efficiency and reduce costs in these processes.

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