Team:Imperial College London/Drylab/Enzyme/Analysis

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<font face='Calibri' size='3'><b>Assumptions</b></font><br><br>

<b>Enzymatic assumptions:</b>
*The enzyme is specific only for the substrate and not for any other chemicals. 
*Only one enzyme, our enzyme of interest is present and participating in the reaction.
*There is negligible formation of product without the enzyme.
*The rate of enzymatic activity remains constant over time because:
**There is no co-operativity of the system. Binding of substrate to one enzyme binding site doesn't influence the affinity or activity of an adjacent site.
**No allosteric regulations from either the product or the substrate.
**There is no product inhibition of the enzyme.


*Total [E] does not change with regards to time. Enzyme will not be used up nor degraded over time, thus [E] at the beginning of the reaction will be the same as [E] at the end of reaction.
*The reaction catalysed is irreversible
*[S] >> [E], such that the free concentration of substrate is very close to the concentration I added. This also ensures a constant substrate concentration throughout the assay. This allows easy determination of [E].
*For which 

[[Image:ek1.jpg]]

, k1>>k2

<br>
<b>Law of mass action assumptions:</b>
*Free diffusion
*Free unrestricted molecular motion
<br>
<b>Michaelis-Menten assumption:</b>
*There is a quasi-steady state of [ES] , ie:  , during which the enzyme is used for the reaction. This means that the rate of formation of ES complex is equal to the rate of dissociation of ES complex.
*	
*from the above assumptions, we know that  


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