. Author manuscript; available in PMC: 2014 Aug 1.

Published in final edited form as: Arch Biochem Biophys. 2013 Jun 5;536(1):72–80. doi: 10.1016/j.abb.2013.05.011

Table 3.

Steady-State Kinetic Parameters for A. baumannii, C. jejuni, and N. gonorrhoeae Acetyltransferase Enzymes

acetyltransferase	substrate	K_m (μM)	k_cat (s⁻¹)	k_cat/K_m (M⁻¹ s⁻¹)
Weel	UDP-4-amino	4300 ± 140	1.1 × 10⁴ ± 1.7 × 10²	2.6 × 10⁶
Weel	AcCoA	110 ± 6.0	3.5 × 10³ ± 5.5 × 10¹	3.2 × 10⁷
PglD	UDP-4-amino	311 ± 23	1.2 × 10⁴ ± 3.8 × 10²	4.0 × 10⁷
PglD	AcCoA	194 ± 30	1.1 × 10⁴ ± 5.0 × 10²	5.5 × 10⁷
PglB-ATD	UDP-4-amino	192 ± 26	2.0 × 10³ ± 8.2 × 10¹	1.0 × 10⁷
PglB-ATD	AcCoA	338 ± 47	2.3 × 10³ ± 1.1 × 10²	6.9 × 10⁶