Application to Mixed Inhibition

FIGURE 1.16 Symbolic representation of the competitive and uncompetitive inhibitions acting through the inhibitor (I) on the enzyme (E) or on enzyme-substrate complex (ES), being quantified by parameters a and a respectively, adjacent to the baseline Michaelis-Menten reaction E+S - ES E+P (Putz Lacrama, 2007). 

In these conditions, the actual working forms for the IT-Lambert and logistic substrate solutions can be immediately generalized from the expressions (1.26) and (1.51) to be  

With these results, we may build the quantum diagrams for the considered t3 es of enzymic reactions by employing the following conceptual-computational algorithm. Firstly, as already considered in treating the mono-substrate case without inhibition, two general rules are considered (Putz Lacrama, 2007 Putz Putz, 2011)  

It follows that the energetic differences as compared with the no-inhibition case are due to the turmeling induced by the inhibited transition states which regulate the delayed times of mixed catalysis. 

An interesting feet is that the no-inhibition case always lies between mixed and some particular case of inhibition, without being at the end sides of the energetic chains of (1.187) and (1.188), as should roughly be presumed. Another observation regards the fact that the competitive and uncompetitive inhibitions change their dominant role in passing from the in vitro to the in vivo circumstances. 

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