At 15mMol I mean it's not defining enzymes inhibition as competitive, non-competitive or un - competitive. Should I go with mixed sort of inhibition mechanism for all???
Or do I need to do kinetic assays again?its km is increasing and at 20mMol it's km is decreasing. What should I do? Should I interpret results accordingly??
Be careful about assuming that all inhibition is due to specific, one-to-one interactions and therefore follows the rules of M-M kinetics. This is especially important for very low-potency inhibitors such as yours (15-20 mM). Examples of non-specific effects include protein denaturation, pH alteration, and formation of inhibitor aggregates to which the protein binds and loses activity.
Also, at lower concentrations, the inhibitor may be well-behaved, but at higher concentrations it may start to show non-specific interactions.
Alternatively, since urease is a multimeric enzyme, there could be cooperativity of inhibitor binding.
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