7)
2
Uncompetitive inhibition typically occurs in reactions with two or more substrates or products
0-15
Non-competitive inhibition is a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate
Inhibitors can prevent a substrate from binding, decrease the enzymes catalytic activity, or do both
This changes the enzymes three-dimensional structure so that its active site can still bind substrate with the usual affinity, but is no longer in the optimal
In fact, at very low substrate concentrations there is minimum inhibition
Competitive inhibition Uncompetitive inhibition Noncompetitive inhibition Answer Bank Vmax remains the same but KM increases Roundup inhibitor binds to the enzyme-substrate complex only KM remains unchanged, but Vmax is lower sulfanilamide lowers Vmax and KM inhibitor and substrate can bind simultaneously doxycycline inhibitor binds at the
Thus the rate should be the same with and without the inhibitor