In noncompetitive inhibition, why does Vmax decrease?
@Somy @Abhisar
@.Sam.
because there is no competition for active site so inhibition of an enzyme is easier & more successful when we deal with competitive one, inhibitor and substrate are competing for the active site of the enzyme, when we increase concentration of the substrate, we are increasing chances of collision between substrate and enzyme, surely with the inhibitor too but overall vmax is more steeply increasing. in case of non competitive inhibition, increasing concentration of the substrate only works in favor of the inhibitor, again increasing chances of successful collisions between each other and that includes inhibitor+enzyme collision. Issue is that since that inhibitor will bind strongly to an enzyme once it gets a hold of it, conc of free enzyme to do the job decreases thereby decreasing the vmax
so what's happening is that the enzyme is like being taken out of the reaction in a way. so It can't reach it's V max
so v max is the maximum velocity the enzyme / substrate can combine? then after that adding more enzyme won't increase the reaction rate?
@Somy
vmax is a maximum velocity at which a reaction is catalyzed using enzymes
so it depends on conditions, is there an inhibitor? what kind? how much is substrate concentration?
http://www.ucl.ac.uk/~ucbcdab/enzass/inhibition.htm this seems like a good source to explain with graphs
key here is you visualization and logic, we both know that for a reaction to take place we need the enzyme and substrate to collide, with good enough KE, which is successful collision. so given that, and also know that one of the inhibitors wants the active site of the enzyme just like a substrate and the other inhibitor can bind to a different section of an enzyme to inhibit it, what can you see?
and then just analyze the situation with increasing and decreasing concentrations of enzyme, inhibitor, substrate
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