Tuberculosis is a pulmonary disease that can be spread through airborne transmission and is one of the leading causes of death worldwide. The success of its causative agent Mycobacterium tuberculosis can be attributed to its metabolic flexibility, giving it an ability to survive within nutrient-poor macrophages. One of the metabolic adaptations include a shift to the glyoxylate shunt in the tricarboxylic acid (TCA) cycle. Many studies have shown that M. tuberculosis uses this shift when grown on fatty acid substrates, or when subjected to antibiotics or hypoxia, all of which are pathologically relevant physiological conditions. This carbon shift is not an all-or-nothing switch but rather a distribution of flux between the glyoxylate shunt and the oxidative branch of the TCA cycle. Studies have shown that a perturbation of this partitioning is detrimental to the bacteria; however, not much is known about the regulation of this flux partitioning. Two enzymes compete for isocitrate in this junction. For the glyoxylate shunt arm, isocitrate lyase catalyses the cleavage of isocitrate to glyoxylate and succinate. For the TCA cycle branch, isocitrate dehydrogenase catalyses the decarboxylation of isocitrate to α-ketoglutarate. This study will focus on isocitrate lyase since humans do not encode orthologues of this enzyme. Specifically, this study aims to identify the protein-level regulation of isocitrate lyase, specifically protein-metabolite interactions and post-translational modifications, in hopes to shed some light on the regulation of this junction.