. Author manuscript; available in PMC: 2009 Jul 6.

Published in final edited form as: J Med Chem. 2008 May 29;51(12):3378–3387. doi: 10.1021/jm7015478

Table 1.

Kinetic parameters and inhibition of wild type and mutated ECE-2s by phosphoramidon^a

Enzymes	K_m(µM)	k_cat(min^-1)	k_cat/K_m (mM^-1 min^-1)	K_i(nM)

ECE-2 WT	5.76±0.55	8.51±1.32	1.48±0.23	1.56±0.23
W148R	3.94±0.15^*	6.84±0.57	1.74±0.15	1.58±0.21
Y563F	6.60±1.37	2.10±0.11^**	0.32±0.02^**	11.07±2.36^***

The kinetic parameters (K_mand k_cat) of the purified enzymes were determined from Michaelis-Menten plots. Inhibition of recombinant enzymes by phosphoramidon (K_i) was determined from dose-dependent inhibition curves for a final McaBk2 concentration of 10μM. Data represent the mean±SEM (n=3).

p<0.05,

^**

p<0.005,

^***

p<0.001.