. Author manuscript; available in PMC: 2012 Oct 18.

Published in final edited form as: Biochemistry. 2011 Sep 21;50(41):8937–8949. doi: 10.1021/bi201181q

Table 1.

Steady-state kinetic constants for BT2127-catalyzed hydrolysis of pyrophosphate and selected phosphate monoesters at 25 °C and pH 7.5 (see Materials and Methods for details).

Substrate	k_cat (s⁻¹)	K_m (mM)	k_cat/K_m (M⁻¹s⁻¹)
pyrophosphate	0.32 ± 0.01	0.0036 ± 0.0004	9 × 10⁴
glycerol 1-phosphate	0.35 ± 0.02	4.8 ± 0.3	7 × 10¹
D-ribose 5-phosphate	0.20 ± 0.02	3.8 ± 0.3	6 × 10¹
fructose 6-phosphate	0.066 ± 0.002	6.4 ± 0.2	1 × 10¹
uridine 5-phosphate	0.15 ± 0.01	2.6 ± 0.4	6 × 10¹
p-nitrophenylphosphate	0.0019 ± 0.0004	0.05 ± 0.01	4 × 10¹