ENZYME KINETICS

1. What are the two basic observations made in the laboratory to study enzyme kinetics?



2. What is the Michaelis-Menten kinetic scheme and how does this explain generally the observed kinetics?





3. Why is the rate of an enzyme-catalysed reaction proportional to the amount of Enzyme-Substrate complex?




4. What is meant by saturation of the enzyme?




5. What is meant by saturation kinetics?




6. How does the formation of an Enzyme-Substrate complex explain the reaching of a maximal velocity in the V
0
vs S
0
graph?




7. Explain mathematically how a value for Km can be obtained from the V
0
vs S
0
graph when V
0
=1/2 V
max
.









8. What is the Michaelis-Menten equation and its Lineweaver-Burk form?




9. How does the Michaelis-Menten equation? Explain why the rate of an enzyme-catalysed reaction is
proportional to the amount of enzyme?




10. How does the Michaelis-Menten equation? Explain why the rate of an enzyme-catalyzed reaction reaches a
maximum value at high substrate?





11. What type of enzyme inhibition does the following graph indicate? What can you say about the chemical
similarities or differences between the substrate and the inhibitor?




ENZYME SPECIFICITY AND CATALYSIS
1. What is the chemical basis of enzyme specificity?





2. Describe generally what an enzyme-substrate complex `looks like





3. What is the chemical basis of enzyme catalysis?







4. What kinds of functional group catalysis by the enzyme is occurring in the following diagram in both the
forward and reverse directions? Indicate clearly what each functional is doing







5. What kinds of functional group would you expect to be involved in the binding of pyridoxal-5-phosphate to
transaminase enzymes requiring this cofactor (derived from Vitamin B6)? Diagram appropriate functional
groups around this cofactor.