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X-Phar410 Part II

Enzymes- Part II

QuestionAnswer
competes with the substrate for the active site of the free enzyme competitive inhibitor; structure often similar to substrate
A reversible competitive inhibitor lowers the effective [S], which increases the measured Km. In other words, it takes more substrate to achieve a half-maximal catalytic rate; v Max stays same because eventually the substrate overwhelm the inhibitor
kM is farther to right; higher reversible competitive inhibition
Lipitor is an example of competitive inhibitor
will only bind the enzyme when the substrate is also bound. It does not bind the free enzyme. An uncompetitive inhibitor
lower vMax is in what kind of inhibitor? uncompetitive inhibitor; increased[S]provides a better target for the inhibitor; not enough [S] will ever overcome this inhibitor
mycophenolate is used to suppress the immune system following organ transplantation in order to minimize the possibility of rejection uncompetitive inhibitor
can bind free enzyme like a competitive inhibitor; but, unlike competitive inhibitors, they do not bind at the active site Mixed inhibitors; can also bind E-S complex like uncompetitive inhibitor
Depending on affinity of I for E or E.S, Km can increase (like a competitive inhibitor) or decrease (like an uncompetitive inhibitor). Mixed (and Pure Noncompetitve) Inhibition
Caspofungin and Foscarnet are examples of what type of inhibitor? mixed
left off on irreversible inhibitors, slide 24
Created by: angieryx