We thus extended our search for alternative cosubstrates of Traboulsi syndrome–associated AspH variants to hydrophobic 2-oxoacids bearing a single carboxylate group, including transamination products of proteinogenic amino acids abundant in cells, because they may stabilize binding to the active site of AspH variants through hydrophobic interactions and because they showed variable levels of activity with bacterial 2OG oxygenases (95, 96). This evidence concerns the gene ASPH and facial dysmorphism-lens dislocation-anterior segment abnormalities-spontaneous filtering blebs syndrome.