non-competitive inhibition

Two types of interaction (competitive or non-competitive inhibition) are allowed.

"The non-competitive inhibition of brain hexokinase by glucose 6-phosphate and related compounds".

Non-competitive inhibition is sometimes thought of as a special case of mixed inhibition.

Non-competitive inhibition models a system where the inhibitor and the substrate may both be bound to the enzyme at any given time.

Both competitive and non-competitive inhibition has been observed for various PGIPs.

Many sources continue to conflate these two terms, or state the definition of allosteric inhibition as the definition for non-competitive inhibition.

Non-competitive inhibition produces plots with the same x-intercept as uninhibited enzyme (K is unaffected) but different slopes and y-intercepts.

Non-competitive inhibition is distinguished from general mixed inhibition in that the inhibitor has an equal affinity for the enzyme and the enzyme-substrate complex.

In non-competitive inhibition, the inhibitor binds to an allosteric site, which alters the active site and makes it inaccessible to the substrate.

This can be competitive inhibition, uncompetitive inhibition, non-competitive inhibition or partially competitive inhibition.

The metalloproteinase inhibitors (MPIs) can prevent unwanted proteolysis by denaturing their target proteases through non-competitive inhibition at an allosteric site.

Non-competitive inhibition of the bacterial homologue LeuT by tricyclic antidepressants resulted from binding of these inhibitors in the extracellular permeation pathway.

The polygalacturonase inhibitor proteins (PGIPs) are leucine-rich repeat proteins that have been reported to demonstrate both competitive and non-competitive inhibition of PGs.

Like HEPT and TIBO, nevirapine blocked viral RT activity by non-competitive inhibition (with respect to dNTP binding).

Non-competitive inhibition is a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate.

The most common mechanism of non-competitive inhibition involves reversible binding of the inhibitor to an allosteric site, but it is possible for the inhibitor to operate via other means including direct binding to the active site.

TBZ, DTBZOH, and KET are thought to exhibit non-competitive inhibition, instead binding to allosteric sites and decreasing the activity of the VMAT rather than simply blocking its substrate binding site.