Hello, you could also try:

http://www.ic50.tk/kmvmax.html

Or

http://ic50.org/kmvmax.html

The former has an exponential decay thing that might help with your substrate 
inhibition and other things if you have biphasic behaviour ;-0

Cheers, Jon.C.

Sent from ProtonMail mobile

-------- Original Message --------
On 18 Jun 2021, 05:04, Prem Prakash wrote:

> Dear all,
> Sorry for this off topic. I am working on an enzyme that has an exonuclease 
> activity. The enzyme preferentially cleaves an unprocessed substrate at a 
> faster rate than the processed one (known by qualitative analysis). Recently, 
> I calculated the Vmax, Km and kcat of the enzyme for unprocessed substrate 
> which are 18.2 pmol/min, 182 nM and 7.1 sec-1 respectively. However, the 
> Processed substrate has apparently a lower range of Km (not calculated) as 
> reflected from the curve (because the same increasing concentration range 
> which is used for unprocessed, shows a steep decline in the initial velocity 
> of the enzyme with processed substrate.
> The latter suggests that Km is way lower than expected. In this case, the 
> question is, if the Km of processed substrate is way lower than the 
> Unprocessed, how can we see a faster rate with the former substrate than 
> later. i.e lower Km and slower rate of cleavage. If it's possible please give 
> some insights. I have attached the plot comparison between two kinetic assays.
>
> With kind regards,
>
> Prem
>
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