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. 2013 Jun 28;288(33):23751–23764. doi: 10.1074/jbc.M113.483289

FIGURE 1.

FIGURE 1.

Steady-state kinetic analysis of TryS. The activities were measured in the in vivo-like buffer system varying the concentration of two substrates while keeping one constant at saturating concentrations. Shown are double reciprocal plots of the reactions with fixed concentrations: 8 mm Spd (A), 2.3 mm ATP (B), and 2.3 mm ATP (C).