Table 4.

Detailed kinetic analysis of reactivation of soman-human AChE mutant Y337A/F338A conjugate by oximes (0.10–3.0 mM). The maximal first-order reactivation rate constant (k₊₂, min⁻¹), the dissociation constant of the phosphylated enzyme-oxime reversible complex (K_OX, μM), and overall second-order reactivation rate constant (k_r, M⁻¹min⁻¹) were determined by nonlinear regression from reactivation data presented in Fig. 4. All constants (± SD), maximal reactivation (React_max, %) and the time in that maximal reactivation was reached (t_max, min), were determined from at least 3 experiments.

Oxime	Kia	KOX	k2	kr	Reactmax	tmax
HI-6	61 ± 12	320 ± 100	1.0 ± 0.12	3300 ± 1000	60	10
RS-170B	21 ± 2	380 ± 60	2.6 ± 0.1	7000 ± 870	63	3
RS-95C	ndb	110 ± 26	0.37 ± 0.02	3500 ± 770	60	15
ICD-585	42 ± 6	100 ± 20	0.14 ± 0.01	1400 ± 300	70	20
HS 6	220 ± 66	320 ± 90	0.23 ± 0.02	710 ± 200	70	30

^adissociation constant of the uninhibited enzyme-oxime reversible complex (K_i, μM) determined in the presence of ATCh (0.05–0.5 mM)

^bnd – not determined