Enzymes- Part II
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| competes with the substrate for the active site of the free enzyme | competitive inhibitor; structure often similar to substrate
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| 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
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| kM is farther to right; higher | reversible competitive inhibition
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| Lipitor is an example of | competitive inhibitor
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| will only bind the enzyme when the substrate is also bound. It does not bind the free enzyme. | An uncompetitive inhibitor
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| 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
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| mycophenolate is used to suppress the immune system following organ transplantation in order to minimize the possibility of rejection | uncompetitive inhibitor
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| 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
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| 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
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| Caspofungin and Foscarnet are examples of what type of inhibitor? | mixed
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| left off on irreversible inhibitors, slide 24 |
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