Fig. 1: The phosphatases mining for catalytic specificity to particular substrates. | Nature Communications

Fig. 1: The phosphatases mining for catalytic specificity to particular substrates.

From: Engineering substrate specificity of HAD phosphatases and multienzyme systems development for the thermodynamic-driven manufacturing sugars

Fig. 1: The phosphatases mining for catalytic specificity to particular substrates.The alternative text for this image may have been generated using AI.

a the screening system for candidate phosphatases using maltodextrin as substrate. Pi: phosphate; Pase was the abbreviation of phosphatases. The reaction system containing 10 g/L of maltodextrin, 10 mM of PBS (pH 6.5), 5 mM of MgCl2. 0.3 mg/mL of TmGP, 0.2 mg/mL of TkPGM, 0.2 mg/mL of DtPGI/MPI, and 60 µL of heat-treated or purified Pases was conducted at 55 °C for 4 h. b The PG/F/M values for different phosphatases were presented. For example, the PM value was calculated by the ratio of mannose concentration to total monosaccharides concentration. PG value indicates the proportion of glucose, and the PF value presents the proportion of fructose. c The SR1/R2 values for Pase1, Pase12 and Pase14. The SM6P/F6P of Pase1 displayed the ratio of activity of Pase1 to M6P over F6P. d The enzyme activity of Pase1 to M6P, Pase12 to G6P and Pase14 to F6P were presented. Data are presented as mean values +/−SD (n = 3 independent experiments). Source data for d are provided as a Source Data file.

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