The , PPP produces nicotinamide adenine dinucleotide phosphate (NADPH), which serves as a hydrogen donor in various biosynthetic processes and has an important role in case of oxidative attack by the infected host. It has also been recognized as an attractive drug target ,and one of its key enzyme is glucose-6-phosphate dehydrogenase (G6PDH). After all, only a limited number of studies are available on enzymes of the PPP (e.g., for parasites and for mammalian homologs, although this pathway is of particular importance. Besides, three-dimensional (3D) structures of the second and third PPP enzymes of T. brucei, the 6-phospho-gluconolactonase (6PGL), and the 6-phosphogluconate dehydrogenase (6PGDH) have been solved. This is particular interest because structural differences between the parasitic and mammalian 6PGDH have been exploited to design molecules that would be specific inhibitors of the T. brucei enzyme.