Enzyme Inhibition Flashcards
a reverse inhibitor is a substance that
binds to an enzyme to inhibit it but can be released (non-covalent bonding)
competitive inhibitors are molecules that
compete with the substrate for binding at the active site of an enzyme
in competitive inhibition, Km
increases
in competitive inhibition, Vmax
unchanged
competitive inhibition can be overcome by
adding more substrate so that the concentration is high enough so that it can outcompete the inhibitor
reason why Vmax is not effected
noncompetitive inhibitors are molecules that
bind at an allosteric site (NOT the active site) and inhibits the enzyme by changing it’s confirmation
in noncompetitive inhibition, Km
unchanged
in noncompetitive inhibition, Vmax
decreases
irreversible inhibition is a
substrate that causes inhibition that cannot be reversed
it usually involves the formation or breaking of covalent bonds to or on the enzyme
tends to be toxic
uncompetitive inhibitors are molecules that
cannot be bound to the enzyme until the substrate has bonded itself on the enzyme
inhibitor only binds to an allosteric site
in uncompetitive inhibition, Km
decreases
in uncompetitive inhibition, Vmax
decreases
mixed-type inhibitors are molecules that
can bind to either the unoccupied enzyme or the enzyme-substrate complex
in mixed-type inhibition, Km
varies
in mixed-type inhibition, Vmax
decreases