Table 1 Kinetic constants for the ATPase activity of selected substrates derived from a Michaelis-Menten type analysis.

The measured ATPase activity is fit to the equation v/[E]T = kcat[S]/(Km + [S]) + kbasal, where v is the measured ATPase activity, [E]T is the total concentration of NaAtm1, [S] is the substrate concentration, and kbasal is the basal rate of ATPase activity, which is measured to be 8.8 ± 0.8 min–1 in 1 mM ATP.

Substratekcat/Km (min–1 mM–1)Km (mM)kcat (min–1)
S-Ag GSH*24000.012 ± 0.00129 ± 1
S-Hg GSH*2000.12 ± 0.0424 ± 1
S-Dinitrobenzene GSH1200.21 ± 0.0526 ± 2
S-Hexyl GSH1000.40 ± 0.1240 ± 4
S-Bimane GSH471.2 ± 0.256 ± 4
GSSG290.97 ± 0.1228 ± 1
GSH3.815 ± 157 ± 2
Glycine2.817 ± 347 ± 4
γ-Glu-Cys2.610 ± 226 ± 2
Ophthalmic acid1.736 ± 562 ± 6
Cys-Gly0.1346 ± 356.2 ± 3.2
Sodium acetate0.1310 ± 211.3 ± 1.2

*Km is reported as per mole of Ag+/Hg2+ basis.