Fig. 3: PGAM1 is phosphorylated and activated by FBP on its catalytic His11. | Nature Communications

Fig. 3: PGAM1 is phosphorylated and activated by FBP on its catalytic His11.

From: Thermal proteome profiling reveals fructose-1,6-bisphosphate as a phosphate donor to activate phosphoglycerate mutase 1

Fig. 3

a Regulations of recombinant PGAM1, PGAM-H11A, PGM1 and PMM2 enzymatic activities by FBP. b Dissociation constants between FBP and recombinant PGAM1, PGM1 and PMM2, measured by microscale thermophoresis (MST). c FBP phosphorylates PGAM1 to form 3-pHis modification by immunoblotting and Phos-tag SDS-PAGE analysis. d Concentration-dependent PGAM1 histidine phosphorylation by 2,3-BPG, PEP and FBP. e Time-dependent PGAM1 histidine phosphorylation by FBP. f LC-MS/MS spectra of histidine phosphorylation at catalytic site His11 of PGAM1. g Immunoblotting analysis and quantification of 3-pHis modification of PGAM1 WT and H11A mutant by FBP treatment. All measurements are presented as mean ± SD for three (a, c, g) or two (b) biological replicates. n = 3 independent experiments with similar results (c, d, e). Statistical differences were determined by a two-sided Student’s t-test. Source data are provided as a Source Data file.

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