. 2012 Feb 17;287(16):13291–13302. doi: 10.1074/jbc.M111.323766

TABLE 1.

Kinetic constants for active JNK1β1 from two-substrate kinetics

Results are the average of at least three independent experiments done in quadruplicate. Errors reported correspond to the mean ± S.E.

Substrate	K_m	k_cat^a	k_cat/K_m
	μm	min⁻¹	μm⁻¹min⁻¹
B-F-ATF2	1.1 ± 0.4	2.2 ± 0.7	3.2 ± 1.3
ATP	6.5 ± 1.3	2.2 ± 0.7	3.2 ± 1.3
H-N-cJun	2.8 ± 0.9	16.8 ± 5.1	6.2 ± 2.1
ATP	4.5 ± 0.1	16.8 ± 5.1	6.2 ± 2.1

^a Enzyme catalytic constant was calculated using the V_max determined from the two-substrate profile and the concentration of the enzyme used in the assay.