How does an enzyme lower the activation energy of a biochemical reaction?
I know the substrate binds to the enzyme, H2O is added to break the alpha 1,4 glycosidic bond, but I still dont get how does this lowers the activation energy
Enzymes lower the activation energy of a reaction by positioning a reactant (or multiple reactants) in very specific conformations and positions. Essentially enzymes are dynamic scaffolds on which reactants are positioned in such a way that the reaction becomes more likely to happen. The activation energy - the energy of the transition state - is lowered, but the relative energies of the reactant(s) and product(s) are not affected. Clear?
What do you mean by positioning the reactant..?? You mean it is place in a different location? or u mean the structure? so can the induced fit model be applied to here?
The reactant binds the enzyme at a very specific site on that enzyme. That site places the reactant in a unique and very specific chemical environment. For example, perhaps a bonding group in the reactant is positioned near a polarizing group in the enzyme. That positioning makes it more likely that the bonding group in the reactant will actually undergo a chemical reaction. The enzyme is a dynamic scaffold. Sometimes binding of the reactant(s) induces a conformational change in the enzyme (the unbound but bindable and fully bound states of the enzyme differ) which make the reaction more likely to happen.
oh ok i get it thanks
Cool. ;D
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