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. 2021 Mar 31;12:643951. doi: 10.3389/fmicb.2021.643951

FIGURE 4.

FIGURE 4

T12 of RmlA is a key residue for activity. (A) Schematic depicting the biochemical reaction catalyzed by RmlA. (B) Phosphorylation detecting with RmlA by PknB coexpression. (C) The activities of RmlA, RmlA-PknB coexpression, and its T12 mutants were determined based on Michaelis–Menten kinetics, representative of three. Five micrograms of purified RmlA protein was added to the 50 μL of enzyme reaction buffer [50 mM Tris (pH 7.5), 1 mM dithiothreitol, 5 mM MgCl2, 0.2 mM dTTP, and 1 mM D-Glc-1-P] and incubation at 37°C for 1 h.