In an allosteric enzyme reaction the shape of the graph is sigmoidal versus a hyperbolic like Michaelis-Menten enzyme. The sigmoidal shape is because the allosteric enzyme has two forms. The T form is when the allosteric enzyme is in its inactive form. The R form is when the allosteric enzyme is in its active form. The allosteric enzyme had multiple subunits in order to make the allosteric enzyme active the binding of a substrate to one subunit of the enzyme is required. Once the substrate binds to a subunit this causing for positive cooperativity to help bind more substrates to the other subunits. This cause the conformational change of all subunits from the T form into the active R form.
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