6-25 For Umax 57(Kr+S) constant an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM b) c) d) e) [S] = 0.5KM [S] = 0.1 KM [S] = 2KM = [S] 10KM Gener (liction)) Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?

3L9

3L6

5) In the below two step transformation, the first step AG is positive i.e. 1.7 kJ/mol. Yet this two step coupled reaction takes place to form Fructose-1.6-bisphosphate. Explain why?" C-H CH-OH CH,-0 H-C-OH AG"- 1.7 KJ/mol (+0.4 kcalmol) C=0 AG"=-14.2 k/mol(-3.4 kcalmol) HO-C-H HO-C-H HO-C-H H-C-OH H-C-OH H-C-OH H-C-OH H-C-OH ATP ADP H-C-OH CH-0-P. CH,-0-P-o- CH,-o- Glucose-6-phosphate Fructose-6-phosphate Fructose-1,6-bisphosphate

In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?

11 X For the hydrolysis of glucose-6-phosphate, glucose-6-P + H₂O = glucose + Pi AG'°= -13.8 kJ/mol and K'eq = 3.81x10-³ at 25°C. Therefore the [glucose-6- phosphate]/[glucose] ratio is about 1/260 at equilibrium. What is the [glucose-6- phosphate]/[glucose] ratio at equilibrium when this reaction is coupled to ATP hydrolysis in the coupled reaction glucose + ATP = glucose-6-phosphate + ADP and [ATP] = ADP]? For ATP hydrolysis AG'°= -30.5 kJ/ mol at 25°C. 0/1 Point Earned 9/10 Attempts Remaining

Can you please help show how to find Kr?