LEGEND TO FIGURES
Figure 1. Simplified kinetic scheme for SucP-catalyzed synthesis of α-D-glucosyl-sn -glycerol (3 ; GlcOG) via transglucosylation from a glucosyl donor (GlcX) to glycerol (GOH). The donor can be sucrose (1 ) or α-D-glucose 1-phosphate (2 ). X is the leaving group.
Figure 2. Kinetic mechanisms considered in this study and experimentally relevant deductions made from them. \(V_{H}\) and \(V_{H2}\) are maximum hydrolysis rates at [GOH] = 0 and glucose is released from E-Glc (mechanisms M1 - M3) and additionally from at E∙∙GlcX (mechanism M2) or E-Glc∙∙GlcX (mechanism M3). \(K_{\text{GlcXH}}\) and \(K_{GlcXH2}\) are binding constants of GlcX to E (mechanisms M1 - M3) or E-Glc (mechanism M3). \(K_{i,GlcX}\) is an inhibition constant for donor substrate.
Figure 3. Results from fitting kinetic mechanisms M1 and M3 to experimental data forLmSucP-catalyzed the transglucosylation from sucrose (Panels 1) and G1P (Panels 2, 3), to glycerol. Experimental data are presented as averages (circles) and corresponding standard deviations (error bars). Solution spaces of resultant fits are shown in red. Effect of changing\(k_{+4}\) (195.15 / 105 s-1) on\(R^{2}\) values is shown. Note, data from Panels D1-3 were not included in the fitting process and compare calculated hydrolysis rates with experimental data. Initial rates of donor group release (X = fructose or phosphate) are indicated by \(v_{X}\) in Panels A, B, C and E, while those of glucose formation are represented by \(v_{\text{Glc}}\) in Panels D and E.
Figure 4 Key results of fits of kinetic mechanism M3 to data for BaSucP-catalyzed transglycosylation. Panel A displays two phasic affinity of G1P toBa SucP determined at 2 M glycerol (\(R^{2}\) = 0.804). Panel B shows transition transfers obtained by linear regression (intercept =1.0) of experimental data (black boxes) and estimated by the M1 (sucrose) or M3 (G1P). The complete data set obtained from parameter estimation analysis can be found in the Supplementary Tables S7 and S8.