inhibitors

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kabuto
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inhibitors

Post by kabuto » Mon Sep 04, 2006 12:52 am

what is the difference between uncompetitive and noncompetitive inhibition??

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mith
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Post by mith » Mon Sep 04, 2006 3:39 am

the binding site I think
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Post by MrMistery » Mon Sep 04, 2006 6:13 pm

Dave is right. In competitive inhibition you have an inhibitor that competes with the active site of the membrane. It is like putting glue in the keyhole of the door. It makes it impossible for you to insert the key.
In non-competitive inhibiton(allosteric inhibition) the inhibitor binds to another site on the enzyme and changes it's shape so that it is no longer able to bind it's substrate. It is like... can't find an analogy...
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mith
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Post by mith » Mon Sep 04, 2006 10:52 pm

the lock is being tickled and it's bent over double :)
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Post by kabuto » Tue Sep 05, 2006 12:33 am

MrMistery wrote:Dave is right. In competitive inhibition you have an inhibitor that competes with the active site of the membrane. It is like putting glue in the keyhole of the door. It makes it impossible for you to insert the key.
In non-competitive inhibiton(allosteric inhibition) the inhibitor binds to another site on the enzyme and changes it's shape so that it is no longer able to bind it's substrate. It is like... can't find an analogy...


how about uncompetitive inhibition??

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Post by herb386 » Tue Sep 05, 2006 7:52 am

Noncompetitive inhibition is when the inhibitor binds to a site on the enzyme away from the ative site. This reduces it's affinity for the substrate and so reduces the reaction rate.

Uncompetitive inhibition is when the inhibitor binds to the enzyme-substrate complex but not the enzyme on it's own.

Have a look at this site for the kinetics:

http://www.chm.davidson.edu/erstevens/L ... eaver.html

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