Question

Physical Origins of Enzyme Catalysis 2. Draw a reaction coordinate diagram for a one step reaction occurring the the absence and present of an enzyme catalyst. Label the x and y axis and indicate which potential energy curve is the enzymatic reaction and which is the non-enzymatic one 3. The following shows the transition state for an enzymatic reaction. Indicate which non- covalent force is contributing to transition state stabilization PHE

Answer 1

Ion It increation. Enzymize the 2: Emayme is biological catalyst for a greaction. It increases the gate of the reaction and does not change after the end of reaction. Enzyme walyst gives a alternative path for the reaction. It stabilizes the transition state and lowess the activation energy for the greaca The reaetion coordinate diagram looks like the following, er without enzyme activation ene without. acetidlion enzyme energy with - V enzyme V- in, Energy rearlants with Enzyme products x Reaction coordinate Hetivation energy with enzyme (activation energy without enzyme. without enzyme is monenzymalicone 3. tranation state is stabilized by diferent non covalent forces line- Change - charge, charge - dipole, dipole - dipole , charge - induced dipole , dipole- induced dipole , london - dispersion force , H-bond, T-t interaction The transition state is induced dipole , london any PHE at For this case it is dipole -induced dipole interaction which gives major stabilization. Along with this london dispersion force also gives weare attractive stabilization. Dipole of Nite functionality creaty a induced dipole in benzenering and stabilizes with dipole- induced dipole interaction. It is shown in the following,