Binding of a molecule at a site other than the active site changes enzyme shape and activity.
Allosteric enzymes have multiple subunits and often show sigmoidal kinetics. Activators stabilise the active form (R state) and inhibitors the inactive form (T state).
This allows fine control at key regulatory steps of pathways.
Binding of a molecule at a site other than the active site changes enzyme shape and activity.
Allosteric Regulation is one of the 51 topics in Biomolecules & Biochemistry. It is rated Advanced, so it suits learners who want specialist depth. Related topics in this area include Induced Fit Model, Quaternary Structure, Cooperativity.
Phosphofructokinase in glycolysis is inhibited by ATP and citrate and activated by AMP.
Work through the Beginner topics in Biomolecules & Biochemistry first, such as Water Properties, Carbon Chemistry, Carbohydrates, then return to Allosteric Regulation. Advanced topics assume the Intermediate vocabulary.
The closest topics to Allosteric Regulation are Induced Fit Model, Quaternary Structure, Cooperativity, Michaelis-Menten Kinetics. Comparing them side by side is a good way to see how the ideas connect.
Read the summary and the in-depth section, then use the quick check on the interactive lesson for Allosteric Regulation. To practise the whole of Biomolecules & Biochemistry, use the Biomolecules & Biochemistry quiz.
Allosteric Regulation: Binding of a molecule at a site other than the active site changes enzyme shape and activity. Induced Fit Model: Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit. Read both side by side and note what each one explains.
First, read the summary and write the definition in your own words. Second, read the in-depth section and note any example. Third, compare it with Induced Fit Model and explain the difference aloud. Finally, take the Biomolecules & Biochemistry quiz and come back to this page for any question you miss.
Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit.
⚗️ Biomolecules & BiochemistryThe arrangement of multiple polypeptide subunits into one functional protein, such as haemoglobin.
⚗️ Biomolecules & BiochemistryBinding of a ligand to one subunit alters affinity at others, giving haemoglobin its sigmoidal oxygen curve.
⚗️ Biomolecules & BiochemistryModels reaction velocity as Vmax times substrate over Km plus substrate, describing enzyme saturation.
⚗️ Biomolecules & Biochemistry