Question

Why are uncompetitive and mixed inhibitors generally considered to be more effective in vivo than competitive inhibitors?

Short answer

In the invivo conditions, the substrate concentration does not vary much and hence they are affected.

Step-by-step solution

Enzyme inhibitors

Through the Michaelis constant KM, a measure of substrate-binding affinity, this equation connects the starting reaction rate (v0), the maximal reaction rate (Vmax), and the initial substrate concentration [S].

Uncompetitive and Mixed inhibitors are more effective invivo than competitive inhibitors

Competitive inhibitors are those that compete directly with the substrate for binding to the enzyme's active site. The enzyme-substrate complex interacts to the uncompetitive inhibitor.

Both free enzyme and the enzyme-substrate complexbind to mixed inhibitors. Competitive inhibitors have an impact that is reliant on the substrate concentration, whereas mixed and noncompetitive inhibitors have an effect that is independent of the substrate concentration. The substrate concentration does not fluctuate significantly in vivo, hence they are unaffected.

The substrate concentration does not fluctuate much under invivocircumstances,therefore they are influenced.

Conclusion

The substrate concentration does not fluctuate much under invivo circumstances, therefore they are influenced.