. Author manuscript; available in PMC: 2014 Jul 7.

Published in final edited form as: Nat Struct Mol Biol. 2013 Dec 8;21(1):36–42. doi: 10.1038/nsmb.2717

Table 1.

Modulation of glucokinase kinetic parameters by BAD BH3 stapled peptides

Treatment	S_0.5 (mM)	V_max (% veh.)	n _H	S_{0.5 Veh}/S_{0.5 Treat}
Vehicle	7.49 ± 0.18	100	1.61 ± 0.03	1.00 ± 0.05	n = 18
GKA (RO0281675)	1.62 ± 0.13^***	138 ± 6.15^***	1.71 ± 0.06	4.62 ± 0.47^***	n = 6
BAD SAHB_A (S118D)	6.54 ± 0.15^**	144 ± 4.64^***	1.71 ± 0.03	1.15 ± 0.05	n = 18
BAD SAHB_A (S118pS)	6.00 ± 0.68^**	129 ± 6.54^**	1.69 ± 0.18	1.25 ± 0.17	n = 3
BAD SAHB_A (S118L)	8.14 ± 0.41	89.6 ± 5.01	1.62 ± 0.05	0.92 ± 0.07	n = 7
BAD SAHB_A (S118D) + GKA	1.35 ± 0.07^***	124 ± 1.54^*	1.84 ± 0.07^*	5.55 ± 0.41^***	n = 4

Summary of the effects of BAD BH3 stapled peptides on GK activity. Kinetic parameters were derived using the Hill equation as described in Methods. S_{0.5 Veh}/S_{0.5 Treat} in the fourth column calculates the fold change in glucose affinity resulting from each treatment. Data represent means ± s.e.m.

P < 0.05,

^**

P < 0.01,

^***

P < 0.001, compared with vehicle control (veh.); one-way ANOVA.