. Author manuscript; available in PMC: 2012 Jun 20.

Published in final edited form as: Biochemistry. 2010 Dec 20;50(2):258–265. doi: 10.1021/bi101622a

Table 2.

Steady-state kinetic parameters and inhibition of LpxC enzymes^a

Species	K_cat (min⁻¹)	K_M (μM)	K_cat/K_M (min⁻¹ μM⁻¹)	K_i (nM)	K_obs^max (min⁻¹)
E. coli	90 ± 2^b	0.19 ± 0.01^b	460 ± 10^b	4.0 ± 1^c	1.9 ± 0.3^c
A. aeolicus	104^e	1.6 ± 0.2^d	65 ± 11^b	1.0 – 1.7^d	0.19^d
Y. enterocolitica	104 ± 3^f	0.40 ± 0.05^f	260 ± 24^f	0.54 ± 0.14^f	0.11 ± 0.01^f

All steady-state parameters and inhibition constants reported were measured at 30 °C, pH 7.5 as described in Materials and Methods or the works cited.

Adapted from reference 14.

Adapted from reference 21. In this species, k₆ is significant, and the overall inhibition constant, K_i*, is 0.4 ± 0.1 nM.

Adapted from reference 19.

Calculated from published values in references 14 and 19.

This work.