In an experiment with a proteolytic enzyme, solutions of a tripeptide at different concentrations were prepared. A small amount of enzyme (5.0*10-$M) was added to the solutions and their rates were measured, giving the following results: [S] (10-SM) 1.07 2.12 3.33 5.25 6.75 8.35 v (10-SM s-) 1.76 3.24 5.14 8.34 10.10 13.34 Based on this data, determine: a) Michaelis constant and maximum rate, using a Lineweaver-Burk plot. (5 pts) b) Turnover frequency. (4 pts) c) Catalytic efficiency of this enzyme. (4 pts) d) Half-life of the substrate when its initial concentration is 104 M. (4 pts) e) The concentration of the substrate after 15 seconds, if the concentration of the enzyme is doubled and [S]= 2.5*10*M. (5 pts)