. Author manuscript; available in PMC: 2009 Nov 25.

Published in final edited form as: Biochemistry. 2008 Nov 25;47(47):12434–12447. doi: 10.1021/bi801311d

Table 2.

Inhibition kinetic parameters and patterns for the inhibitors of B. anthracis OSB-CoA synthetase^a

Varied substrate	Inhibitors	Fixed substrates (μM)			K_m (μM)	K_i (mM)	αK_i (mM)	Inhibition pattern
Varied substrate	Inhibitors	OSB	ATP	CoA	K_m (μM)	K_i (mM)	αK_i (mM)	Inhibition pattern
ATP	AMP	8	-	128	13.1 ± 1.0	3.6 ± 0.4	-	competitive
CoA	AMP	8	16	-	49.9 ± 4.9	-	10.3 ± 0.6	uncompetitive
OSB	AMP	-	16	128	2.8 ± 0.2	4.6 ± 0.6	34.5 ± 4.5	mixed
CoA	Benzoyl-CoA	8	16	-	66.2 ± 6.3	3.0 ± 0.5	15.3 ± 2.6	mixed
CoA	TFMP-butyl-AMS	8	16	-	39.3 ± 1.8	-	0.0089 ± 0.0005	uncompetitive
ATP	TFMP-butyl-AMS	8	-	128	5.4 ± 0.5	0.0052 ± 0.0008	0.108 ± 0.017	mixed
OSB	TFMP-butyl-AMS	-	16	128	3.6 ± 0.2	0.0056 ± 0.0008	0.025 ± 0.004	mixed

Data presented as mean ± standard error in the fit parameters