Talk:Non-competitive inhibition

message: I'm not sure that it is correct to call non competitive inhibition allosteric.  Certainly they are similar with regard to the inhibitor (and activator in the case of allosteric enzymes) binding to a site other than the active site.  however, allosteric mechanisms will change the Km whereas non competitive do not change the km.  They are different classes of inhibition by definition.  David D. (Talk) 04:48, 30 August 2005 (UTC)
thread_title: organophosphate insecticides are non-competitive at active site, right?

message: There are some discrepancies in the entries about inhibition, causing great (at least to me) confusion:
My book (Lehningers principles of biochemistry) state that a mixed inhibitor has been classically defined a noncompetitive inhibitior. Here there are two diffrent entries. Could anyone clariffy? —Preceding unsigned comment added by Leonidaslundell (talk • contribs) 
:Many text books have it wrong. By definition a noncompetitive inhibitor changes the Vmax, not the Km, and is reversible. Mixed inhibitors typically cause changes to an enzymes Vmax and Km. In fact, there are very few examples of non-competitive inhibitors.  As far as i can tell the only reason they are useful with regard to text books is to contrast with competitive inhibitors that change the Km but not the Vmax (exact opposite of non-competitive). Suicide inhibitors are similar to noncompetitive but the fail on the important criteria of being reversible. I suspect what Lehninger is tacitly admiting is that there are no real noncompetitive inhibitors and the closest are mixed inhibitors that have very subtle changes in Km but large changes in Vmax. A better book to read up on this stuff is Biochemical Calculations by Irwin H. Segal. I hope this helps David D. (Talk) 14:58, 15 September 2006 (UTC)
thread_title:  Confusion 

message: It is wrong to define inhibition types based on hypothetical mechanisms. The fact is that non-competitive inhibition is any type of inhibition that causes the apparent limiting rate (Vmax) to decrease without affecting Km. Whether this happens through binding to some other site, or by changing conformation, or by altering electrostatic distribituin, etc. is irrelevant. This article is damaging to education by promoting an erroneous concept. (Yes, the mechanism proposed in the article could lead to non-competitive inhibition but it is a special case)  —Preceding unsigned comment added by 86.133.61.88 (talk) 09:02, 26 September 2010 (UTC)
thread_title: Wrong approach

message: Our group was assigned to add a history section to non-competitive inhibition.  
We are looking at: what enzyme the founders were using when they discovered it, the founders along with a bit on their early life, if it was discovered during a Ph.D thesis, and what experiment they were performing to discover it.  We believe that history is appreciation.  Knowing how something is discovered, when and for what reason could aid future scientists to possibly use in their research.
Allisonbcookie (talk) 23:28, 9 October 2017 (UTC)
thread_title:  Possibly Adding History of Non-competitive inhibition 

message: Our group was assigned the mechanism section of non-competitive inhibition. We intend to add practical examples of non-competitive inhibition, distinguish the difference between non-competitive and competitive inhibition, and a description of the kinetics of non-competitive inhibition in terms of Km and Vmax. AMars1997 (talk) 01:28, 13 October 2017 (UTC)
thread_title:  Editing Mechanism Section