Table 2. Kinetic Parameters of the Bacterial DPP7 and DPP11 toward Synthetic Substrates Measured in Bulk^a.

enzymes	substrates	Vmax (IU mg–1)	Km (μM)	kcat (s–1)	kcat/Km (μM–1 s–1)	ratio of kcat/Km to AMC
PmDAPBII	Met–Leu–AMC	0.637 ± 0.012	5.30 ± 0.12	0.811 ± 0.016	0.153 ± 0.004	1.00
	Met–Leu–ACA	0.483 ± 0.002	1.11 ± 0.02	0.614 ± 0.003	0.552 ± 0.005	3.60
SmDPP7	Met–Leu–AMC	0.672 ± 0.006	21.1 ± 0.5	0.849 ± 0.007	0.0402 ± 0.0007	1.00
	Met–Leu–ACA	0.512 ± 0.003	4.09 ± 0.13	0.647 ± 0.004	0.158 ± 0.004	3.94
PgDPP11	Leu–Asp–AMC	3.93 ± 0.06	10.6 ± 0.2	5.22 ± 0.08	0.492 ± 0.007	1.00
	Leu–Asp–ACA	2.94 ± 0.07	10.1 ± 0.5	3.90 ± 0.10	0.386 ± 0.008	0.785
SmDPP11	Leu–Asp–AMC	14.3 ± 0.4	45.0 ± 1.9	18.0 ± 0.5	0.401 ± 0.007	1.00
	Leu–Asp–ACA	18.1 ± 0.3	12.2 ± 0.4	22.8 ± 0.3	1.88 ± 0.03	4.68

^aStandard deviations were obtained from three independent experiments. Michaelis–Menten plots are shown in Figure S8.