What does uncompetitive inhibition in the enzyme-substrate reaction tells us
Uncompetitive inhibition occurs when inhibitor binds only enzyme-substrate complex, not free enzyme, at allosteric site distinct from active site. Binding requires prior substrate attachment forming ES-I dead-end complex. This reduces both Vmax and Km, unlike competitive inhibition competing for catalytic site.
Ref: Nelson and Cox, Lehninger Principles of Biochemistry, 7th Edition, Chapter 6 Enzyme Kinetics and Inhibition, describes uncompetitive inhibition inhibitor binds only enzyme substrate complex ES not free enzyme allosteric site reduced Vmax Km formation of dead end ESI complex, published by W.H. Freeman.