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

FIGURE 3.

FIGURE 3.

Product inhibition of TryS by T(SH)2. The assays were conducted in the in vivo-like buffer system. The reaction mixtures contained in the presence or absence of T(SH)2 0.2 mm GSH, 2.3 mm ATP, and variable Spd concentrations (A), 0.2 mm GSH, 2.3 mm ATP, and variable Gsp concentrations (B), 8 mm Spd, 2.3 mm ATP, and variable GSH concentrations (C), and 0.52 mm Gsp, 2.3 mm ATP, and variable GSH concentrations (D). Data in A and B were fitted to the Michaelis-Menten equation. The kinetic constants derived are given below the graphs. Data in C and D were fitted to the high substrate inhibition equation (solid lines) and for the highest T(SH)2 concentration also to the Michaelis-Menten equation (dashed line).