The combined observations indicate that the reactivity of abundant hydrophobic amino acid transamination products with pathogenic AspH variants differs from that of 2OG derivatives and that these types of 2-oxoacids have the potential to sustain catalysis of Traboulsi syndrome–associated AspH variants in cells. This evidence concerns the gene ASPH and facial dysmorphism-lens dislocation-anterior segment abnormalities-spontaneous filtering blebs syndrome.