Fig. 3: Characterization of the enzyme activity and protein expression of all previously reported FBP1 missense mutations. | Communications Biology

Fig. 3: Characterization of the enzyme activity and protein expression of all previously reported FBP1 missense mutations.

From: Identification of genotype–biochemical phenotype correlations associated with fructose 1,6-bisphosphatase deficiency

Fig. 3

a Schematic distribution of all previously reported FBP1 missense mutations. Substrate binding site, metal binding site, and AMP binding sites are shown according to the NCBI and UniProt databases. b FBPase enzyme activity of all FBP1 missense mutants. All these mutants, except for G207R and V325A (NS: not significant), exhibited a loss in enzymatic activity (**P < 0.01 versus WT) (one-way ANOVA test followed by Dunnett’s multiple comparison test). The data are presented as the mean ± SD; n = 6–12. c, d Protein expression of all FBP1 missense mutants in FBP1-KO HepG2 cells. All the mutants that did not change their hydrophobicity, except for G294V, exhibited sufficient protein expression compared with that of WT FBP1, whereas all the mutants that changed their hydrophobicity, except for G207R, exhibited decreased protein expression. The data are presented as the mean ± SD. **P < 0.01 versus WT (one-way ANOVA test followed by Dunnett’s multiple comparison test) (n = 3–4). Vertically stacked strips of bands in a figure were evaluated in the same experimental conditions respectively while they were not in fact all derived from the same gel.

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