Phosphopantetheine transferase (PptT) is an essential enzyme in M. tuberculosis that transfers a phosphopantetheine with its free sulhydryl onto the apo-forms of multiple acylcarrier proteins. The resulting holo-acylcarrier proteins are enzymes that M. tb needs to make both its structural lipids called mycolates, its virulence lipids, and siderophores (small, high-affinity iron-chelating molecules that help TB acquire iron from its mammalian host). Through an indirect action, inhibitors of PptT also suppress M. tb's levels of coenzyme A. Potent whole cell active compounds have been identified and lead identification efforts are focused on understanding and optimizing their oral bioavailability.