. 2018 Nov 12;58(5):391–400. doi: 10.1021/acs.biochem.8b00858

Table 3. Michaelis–Menten Constants for Selected A3 Enzymes and Mutants Measured by the NMR Assay^32,40.

protein	substrate	k_cat (s^–1)	K_m (μM)	k_cat/K_m (s^–1 μM^–1)
A3G_CTD^a	Oligo-3	0.10 ± 0.04	570 ± 90	0.00018
A3A^b	Oligo-2	1.2 ± 0.1	66 ± 7	0.018
A3B_CTD-QM-ΔL3-AL1swap^c	Oligo-2	0.28 ± 0.04	200 ± 30	0.0014
A3B_CTD-DM^c	Oligo-2	0.008 ± 0.001	320 ± 60	0.000025
A3B_CTD-QM-ΔL3^c	barely active

See ref (32).

Table 3. Michaelis–Menten Constants for Selected A3 Enzymes and Mutants Measured by the NMR Assay32,40.