"Ping-Pong" mechanism

Question

After enolase, the enzyme just after phosphoglycerate mutase in the glycolytic pathway, the next enzyme is pyruvate kinase (PK). This enzyme is the last enzyme in the pathway and transfers phosphate from phosphoenolpyruvate (PEP) to ADP, making ATP. It catalyzes this reaction:
PEP  +  ADP   ->  pyruvate  +  ATP	
You wish to characterize PK from Staphylococcus sp. ATCC7893 as well, because it is a key step in making ATP.  To do this, you set up 25 tubes containing buffer (pH 7.4), ions (to mimic the intracellular environment), and various combinations of PEP and ADP. You initiate each reaction by adding pyruvate kinase (final concentration = 1 nM), stop it 1 minute later, and then measure the concentration of ATP produced using a sensitive luminescence assay. From this data, you estimate the initial rate of the reaction in each tube, which is tabulated below:
[PEP]
(µM)	initial velocity (nM/s)  when [ADP]  (mM) =
	0.2	0.6	1.8	5.4	16.2
2	0.255	0.686	1.7	3.2	4.81
6	0.693	1.95	4.61	8.6	11.6
18	1.73	4.77	10.3	18.2	23.8
54	3.3	8.62	18.6	30.5	35.9
162	4.92	11.9	25.3	37.8	44.7

Which of these enzymatic mechanisms is most consistent with these data?
a) "Ping-Pong" mechanism
b) ternary complex with ordered pathway (which one binds first?)
c) ternary complex with random pathway

Briefly justify your conclusion.  
		
Determine the following parameters for this thioredoxin reductase enzyme:
Km and/or Kd for ADP
Km and/or Kd for PEP
kcat of the enzyme 
Note: For full credit on this problem, you must show all work. If you used an Excel spreadsheet, you must attach this, and it must be clearly annotated.  (i.e., it should say what each calculation is doing, what the units are for each associated number, etc.)