Table 3.

Kinetic Parameters for Activators of the D-GpNA Hydrolysis Reaction and Inhibition of the L-GpNA Transpeptidation Reaction.

		Hydrolysis D-GpNA				Inhibition L-GpNA
Compound #	Substitution	Voa (mM/min/nM)	V∞ (mM/min/nM)	KAct (μM)	Fold Activation	Transpeptidation L-GpNA Kii (μM)	Transpeptidation glygly Kis (μM)
13	None	1.59 ± 0.06	9.09 ± 0.55	54.4 ± 3.0	5.72 ± 0.32	111.5 ± 5.5	59.6 ± 3.7
14	Y = NO2	1.27 ± 0.01	5.08 ± 0.41	51.9 ± 0.8	4.00 ± 0.11	132.5 ± 5.5	81.2 ± 8.8
15	Z = Cl	1.30 ± 0.01	5.86 ± 0.23	38.6 ± 0.3	4.51 ± 0.05	119.1 ± 7.1	43.8 ± 7.7
11b	Y = OCH3	1.59 ± 0.14	8.63 ± 1.21	37.1 ± 5.6	5.43 ± 2.04	92.8 ± 4.3	95.7 ± 7.6
16	Y = Cl	1.71 ± 0.09	7.70 ± 0.46	31.4 ± 2.2	4.50 ± 0.63	61.9 ± 2.4	44.4 ± 3.4
17	Y = CH3	2.62 ± 0.79	11.25 ± 4.27	25.3 ± 7.6	4.29 ± 2.20	112.5 ± 5.2	56.9 ± 8.3
18	Z = CH3	1.15 ± 0.01	5.08 ± 0.20	25.2 ± 0.2	4.42 ± 0.64	121.5 ± 8.8	34.3 ± 0.9
19	Y = F	1.53 ± 0.09	5.39 ± 0.28	22.2 ± 2.0	3.52 ± 0.60	Time Dependent	31.8 ± 0.7
20c	Y = Cl Z = Cl	--	--	--	--	Time Dependent	10.3 ± 0.5

^aV_o = maximum velocity at zero activator; V_∞ = V_o(K_ID/K_IN) in eq. 2, maximum rate at infinite activator; K_act, activation constant or concentration that gives ½(V_∞ + V_o), K_ID in eq. 2; fold activation = V_∞/V_o.

^bNormalization of all values to Compound 11 yielded values similar to Compound 11

^cCompound 20 competitively inhibited the hydrolysis reaction with a K_ii with D-GpNA of 78.2 ± 1.9 μM.