Fig. 5: Structure-activity relationship studies of FBP-PGAM1 interaction. | Nature Communications

Fig. 5: Structure-activity relationship studies of FBP-PGAM1 interaction.

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

Fig. 5

a Chemical structures of endogenous sugar phosphates including FBP, F1P, F6P, M1P, M6P, GBP, G1P, G6P and 2,3-BPG. b Immunoblotting and Phos-tag SDS-PAGE analysis of PGAM1 phosphorylation by bisphosphates FBP, GBP, 2,3-BPG compared with monophosphates F1P, F6P, G1P, G6P, M1P and M6P. c Enzymatic assay of PGAM1 treated by various sugar phosphates. d Design of FBP analogues α-MeFBP, β-MeFBP, 4-dexoyFBP, 1-DMeFBP, 6-DMeFBP and 1,6-DMeFBP based on the molecular insight of FBP-PGAM1 interaction. e Immunoblotting and Phos-tag SDS-PAGE analysis of PGAM1 histidine phosphorylation by FBP and its synthetic analogues. f Enzymatic assay of PGAM1 treated by FBP and its synthetic analogues. g IC50 of PGAM inhibition by synthetic FBP analogues 1-DMeFBP, 6-DMeFBP and 1,6-DMeFBP. All measurements are presented as mean ± SD for three biological replicates. Statistical differences were determined by one-way ANOVA followed by Dunnett’s multiple comparison tests. ****P < 0.0001, n.s. P > 0.5. Source data are provided as a Source Data file.

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