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allosteric site
This term is a specialized technical expression used almost exclusively in biochemistry and molecular biology. It describes a regulatory mechanism where the binding of an effector molecule at one location on a protein affects the binding or catalytic properties at a different, distant location. This distinguishes it from competitive inhibition, where a molecule competes for the same active site.
In a laboratory or academic context, the term is used to explain the "switching" behavior of enzymes, where the protein transitions between an active and an inactive state. It is a precise descriptor of spatial and functional separation within a single macromolecule.
Meanings
Examples
The inhibitor binds to the allosteric site to reduce the enzyme activity.
Wait, does this molecule target the active site or the allosteric site?
Binding at the allosteric site triggers a conformational change in the protein.
We need to design a drug that specifically targets the allosteric site for better selectivity.
We need to design a drug that specifically targets the allosteric site for better selectivity.
The effector molecule attaches to the allosteric site to increase substrate affinity.
I wonder if modifying the allosteric site would stabilize the R state of the enzyme.
The regulatory subunit contains a distinct allosteric site for ATP binding.
The regulatory subunit contains a distinct allosteric site for ATP binding.
Noncompetitive inhibitors typically act by binding to an allosteric site.