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Competitive Inhibition
def: the inhibitor structurally resembles the substrate and competes for the same active site on the free enzyme
binds to E complex
inhibitor can be overcome if a big amount of substrate is added
Vmax= Unchanged
Kmax= Increased
lines intersect on the y-axis

Noncompetitive Inhibition
def: the inhibitor binds to a different site (allosteric site), not the active site
can bind to the E complex or ES complex
can not be overcome since substrate binding is not inhibited, so Vmax is permanently reduced
Vmax= Decreased
Km= Unchanged
lines intersect on the x-axis

Uncompetitive Inhibition
def: inhibitor only binds to the ES complex, NEVER THE FREE ENZYME
when the substrate binds to the active sire, it causes a conformational change in the enzyme, then the inhibitor recognizes and binds to the newly exposed site on the enzyme
inhibition increases when more substrate is added since ES formation would increase; giving the inhibit more target to bind to
same slopes and both intercepts change proportionally
Vmax= DECREASES
Km= DECREASES

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