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This inhibition may follow the competitive, uncompetitive or mixed patterns. In substrate inhibition there is a progressive decrease in activity at high substrate concentrations, potentially from an enzyme having two competing substrate-binding sites. At low substrate, the high-affinity site is occupied and normal kinetics are followed.
Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works. This can be competitive inhibition, uncompetitive inhibition, non-competitive inhibition or partially competitive inhibition.
During competitive inhibition, the inhibitor and substrate compete for the active site. The active site is a region on an enzyme to which a particular protein or substrate can bind. The active site will thus only allow one of the two complexes to bind to the site, either allowing a reaction to occur or yielding it.
Contact inhibition is a regulatory mechanism that functions to keep cells growing into a layer one cell thick (a monolayer). If a cell has plenty of available substrate space, it replicates rapidly and moves freely.
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. [1] This is unlike competitive inhibition, where binding affinity for the substrate in the enzyme is decreased in the presence of an inhibitor.
K i is the inhibition constant for a drug; the concentration of competing ligand in a competition assay which would occupy 50% of the receptors if no ligand were present. [ 5 ] The Cheng-Prusoff equation produces good estimates at high agonist concentrations, but over- or under-estimates K i at low agonist concentrations.
Product inhibition is a type of enzyme inhibition where the product of an enzyme reaction inhibits its production. [1] Cells utilize product inhibition to regulate of metabolism as a form of negative feedback controlling metabolic pathways . [ 2 ]
Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.