Table 1.

Inhibition of IMPDHs by compounds A–H. These compounds (100 µM) do not inhibit EcIMPDH, TfIMPDH and LdIMPDH. The errors on the IC₅₀ values were less than 10% unless otherwise noted. "Intrinsic" values (adjusted for the fraction of enzyme in the open conformation) are shown in parentheses.

Compound	IC50(µM)
	CpIMPDHa	HpIMPDH	BbIMPDH	SpIMPDH	EcIMPDH- S250A/L444Y
	3.3 0.66	2.2 1.1	1.4 0.84	96 12	1.8 0.54
	1.6 0.32	1.3 0.65	1.8 1.1	85 11	0.70 0.21
	1.2 0.24	0.60 0.30	0.60 0.36	70 9.1	0.60 0.18
	5.4 1.1	3.0 1.5	1.7 1.0	49 6.4	2.3 0.69
	1.6 0.32	1.5 0.75	0.90 0.54	15 2.0	1.8 0.54
	1.4 0.28	1.1 0.55	0.80 0.48	13 1.7	1.1 0.33
	0.1 0.02	0.30 0.15	0.22 0.13	0.55 0.07	0.40 0.12
	0.9 0.18	1.2 0.6	0.90 0.54	0.86 0.11	1.0 0.3
	0.008b, c 0.0016	0.0011b, e 0.0005	n.d.	0.0054b, c 0.0007	0.0019b, f 0.0006

^adata from (Umejiego, et al., 2008);

^bdetermined with a tight-binding equation;

^cerror ≤ 37%.

^derror = 73%; error = 52%. Supported by Figure S1.