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X-Phar410 Part II
Enzymes- Part II
| Question | Answer |
|---|---|
| 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
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