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. 1999 Jan 5;96(1):44–48. doi: 10.1073/pnas.96.1.44

Table 1.

Determined kinetic constants for the selenophosphate synthetase enzymes

Selenophosphate synthetase Km ATP, mM Km selenide, μM Specific activity, nmol/min per mg
E. coli 0.9 20 29
H. influenzae 1.3 25 16

Reactions were performed anaerobically at 37°C. Reaction mixtures (0.1 ml) contained 100 mM Tricine⋅KOH (pH 7.8), 2 mM DTT, 20 mM KCl, 4 mM MgCl2, 5 μM selenophosphate synthetase, and the appropriate concentration of substrate.