dttom Posted October 7, 2009 Posted October 7, 2009 I was told that for an allosteric enzyme regulation to work, the enzyme in account should contain at least 2 subunits, but I can't understand why this is necessary. I think enzyme regulation is different from competitive inhibition as the former just stabilize the T state shifting the equilibrium but not directly competing for active site as in the latter case. And I think enzyme regulation is also different from non-competitive inhibition as non-competitive inhibition directly bind and inhibit the R state while the former just stabilize the T state, so it is in an equilibrium, an increase in substrate concentration could shift back the equilibrium. But this is not the case in non-competitive inhibition as the inhibitor also binds with the enzyme-substrate complex, a certain amount of active ingredient are definitely inactivated. I don't know these two understandings are correct or not. When I try to explain it by that, 'the enzyme must have at least 2 subunits as the binding of regulator would not directly affect the polypeptide chain containing the active site', this explanation should fail as I can't see any reason that a regulator binding to an allosteric site of an enzyme with single chain only when the enzyme is in T state could make any difference from an enzyme with 2 chains (subunits). I hope there are somebody to answer my question... even discuss is helpful... Thanks.
CharonY Posted October 7, 2009 Posted October 7, 2009 Actually it is easy. You have to think more in terms of mechanism. On which part does a competitive inhibitor bind on the enzyme, and where doe allosteric inhibitors bind?
dttom Posted October 8, 2009 Author Posted October 8, 2009 A competitive inhibitor binds directly to the active site and an allosteric one binds to an allosteric site away from the active site, both of them bind the enzyme in R state. So is the binding to R state by these inhibitor but the binding to T state of those regulators what make a difference? And why single chain protein, assuming it does have an allosteric binding site and flipping between T and R states, not be effective in regulation by these regulators?
CharonY Posted October 8, 2009 Posted October 8, 2009 Wait a tick, I may have misunderstood your question. Are asking whether several subunits (i.e. protomers) are needed? The latter is dependent a bit on what model for allosteric inhibition is used.
dttom Posted October 9, 2009 Author Posted October 9, 2009 Yes the question is about whether polysubunit is needed. But it focuses on regulation rather than inhibition. I think regulation is different from inhibition that regulator binds to T state but allosteric inhibitor binds to R state. (otherwise regulator would have a lower max. reaction velocity, but the max. velocity remains in fact)
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