Do enzymes form more weak non-covalent interactions with the substrate, transiti

Question

Do enzymes form more weak non-covalent interactions with the substrate, transition state, or product? Explain. 2.On a free energy diagram: Distinguish between an intermediate and a transition state Show the effect of an enzyme on the transition state Point out each of the following on a free energy diagram, showing the a. C. effect of the presence of an enzyme: a) activation energy for forward reaction b)activation energy for reverse reaction c) value of rate limiting rate constant for forward reaction d)value of rate limiting rate constant for reverse reaction e) AG Use a free energy diagram to show whether the value for Keq will be d. greater or less than one e. Use a free energy diagram to show whether the value of AG will be positive or negative For a reaction that has a negative AG, will the reaction always proceed quickly toward product formation? Why, or why not? 3.Give a brief description of how each of the following contribute to catalysis a.general acid/base catalysis covalent catalysis c. metal ion catalysis 4. a.With correctly labeled axes, draw a Michaelis-Menten plot. Show how this plot can be used to determine Km and Vmax.

Explanation / Answer

Ans.1 Enzymes form weak non covalent interactions with the substrate.Enzyme contain a small active site which form bond with substrate and carries a reaction. Active site has catalytic group which is responsible for formation and breaking of bonds. By breaking and formation enzyme and substrate interaction result in transition state formation. Active site of enzyme promotes the formation of weak interaction due to its non polar microenvironment.Each enzyme binds to specific substrate and this complementary shapes of enzyme and substrate enhance the formation of weak non covalent interaction such as electrostatic force,hydrogen bond etc.So enzyme form non covalent interaction with substrate.

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