Fig. 1: MsmIMPDH is regulated by both GTP and ppGpp in an ATP-dependent manner.
From: Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase
a, c Initial velocity, fitted with the Hill equation, is plotted as a function of IMP concentration in the presence of 500 µM ATP and varied concentrations of (a) GTP and (c) ppGpp, respectively (n = 3). Control kinetics in the presence of 500 µM ATP only are shown in black dashed line. b, d Relative velocity is plotted as a function of the ATP concentration at set concentrations of (b) GTP and (d) ppGpp (n = 2). The substrates IMP and NAD+ were fixed at concentrations of 100 µM and 2 mM, respectively. The relative velocity value was calculated as the ratio of the initial velocity of the reaction in the presence of ATP and GTP or ATP and ppGpp to the control reaction containing only the substrates and the corresponding ATP concentration. Specific ATP concentration ranges above the graphs indicate where inhibition and reactivation occur. All data are presented as mean values with error bars representing the SD.
