Malaria is a deadly disease that claims the lives of almost half a million individuals worldwide annually and is caused by Plasmodium parasites, most significantly Plasmodium falciparum. Unfortunately, resistance now exists against all currently available therapies. Therefore, there is an urgent need for the development of novel therapeutics and insight into the biochemical processes of this parasite may reveal potential drug targets. Inside erythrocytes the parasite rapidly replicates asexually, requiring the rapid utilisation of energy and synthesis of macromolecules. The pentose phosphate pathway is a branch of glucose metabolism that supports this growth through two distinct phases: the oxidative phase and the non-oxidative phase. Whilst there is clear evidence for a pentose phosphate pathway in Plasmodium, the majority of enzymes involved are uncharacterised. Genome annotations suggest the presence of all enzymes of these pathways with the notable exception of transaldolase. Transketolase-transaldolase coupled reactions are thought to be fundamental to the non-oxidative phase which begs the question- is a transaldolase present or is a non-canonical pathway at play? We inducibly knocked down and knocked out the enzymes 6-phosphogluconate dehydrogenase (6-PGDH) and transketolase (TKL) from the oxidative and non-oxidative phases of the pentose phosphate pathway, respectively. We show that while 6-PGDH is essential for parasite viability, TKL is not. Metabolomic experiments confirm activity of both oxidative and non oxidative branches of the pentose phosphate pathway in Plasmodium, as well as indicating a non-canonical metabolic bypass of the missing transaldolase.