In the field on enzymology, you will find yourself investigating the kinetics of an enzyme-catalyzed reaction. If you wrongly assume that this reaction behaves "Michaelis-Menten like" (i.e., among others, that it will go towards full conversion), you might observe what you think is inhibition. This "inhibition" might be an artifact generated by the reaction being actually reversible, and the underlying thermodynamics that will fool you.
Take this for example: If you want to characterize a reaction
A + ZH <=> AH + Z
you determine K_M for substrate "A", while keeping the concentration of ZH high enough ("saturated"). However, if ZH is NADH, you want to keep it low because it's pricy. Let's assume you take ZH = 2 mM. If you now determine the "inhibition effect" of AH or Z, you might add a lot of it. At some point, you will move the equilibrium to the left by the massive amounts of AH or Z, which could even look like negative velocity.
You are interested in this topic? But the idea is gibberish and incomplete, or non-sense? Well, you're probably right!
All of this is work in progress -- I would be very happy if you get in touch so we can improve this!
You are free to use this idea in whatever way you like. I put this material under CC-BY license, just to make it legally clear, but: "Gedanken sind frei" (ideas are free) -- I don't expect them to be protectable anyway.
This "Farm of Ideas" is supposed to store ideas I would like to develop into scientific progress some day, and to store their progression from initial idea being had, over keeping them alive, to growing them into something real and then "harvesting".
If you are faster in developing them, I am happy with you and for the world! :) Just to avoid me having spend time on something you already realized then, I would be grateful for a short letting-me-know email.