Fig. 4

Analysis of the PI4KA Protein Homology and Enzyme Activity. (A) Comparison of PI4KA protein homology at the position of amino acid A940. The alignment depicts the conservation of amino acid A940 across various species. (B) Predicted 3D structure of the wild type (WT) and mutant (c.2819 C > T, p.Ala940Val) PI4KA proteins. The structures, generated using the Swiss-Model website, illustrate the potential conformational changes due to the p.Ala940Val mutation. (C) Purification of the wild type and p.Ala940Val mutant form of the PI4KA enzyme. (D) Enzyme activity assay for the wild type and p.Ala940Val mutant PI4KA enzymes. The plot compares the catalytic activities of the WT and mutant enzymes, with the ptt5 plasmid used as a negative control. The results indicate a marked decrease in the catalytic activity of the mutant enzyme (p.Ala940Val) relative to the WT enzyme. The experiments were performed in triplicate