Why are uncompetitive and mixed inhibitors generally considered to be more effective in vivo than competitive inhibitors?
In competitive inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time.the substrate and inhibitor compete for access to the enzyme's active site. In vivo, substrate can be constantly made and therefore, the effect of the competitive inhibitors can be diluted out by increasing amounts of substrate. In uncompetitive and mixed inhibition, the inhibitor binds only to the substrate-enzyme complex or when the inhibitor binds to the enzyme alone (mixed inhibitions only). Therefore, it doesn't matter how much substrate is around because these inhibitors bind in a different place.