Fig. 7: Effect of Mn2+ on R32A-PaATPPRT and R56A-PaATPPRT reactions. | Nature Communications

Fig. 7: Effect of Mn2+ on R32A-PaATPPRT and R56A-PaATPPRT reactions.

From: Allosteric rescue of catalytically impaired ATP phosphoribosyltransferase variants links protein dynamics to active-site electrostatic preorganisation

Fig. 7

a PRATP formation time course catalysed by PaHisGS and PaATPPRT variants at fixed, saturating concentration of PRPP and ATP. Traces are averages of two to four independent measurements. Black lines are linear regressions of the data. Source data are provided as a Source Data file. b Apparent first-order rate constants for PaHisGS and PaATPPRT variants. All data points are shown. Two independent measurements were carried out for PaHisGS variants, and four for PaATPPRT. For the latter, where less than four data points are apparent, identical rates for two replicates overlap.

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