Understanding the origin of life remains one of Science's greatest challenges. Enormous progress has been made in discovering plausible prebiotic reaction pathways to the building blocks of life. Nevertheless, with the increasing complexity of the chemical pathways that could have supported the origins of life, comes the realization that prebiotic chemistry lacks the required selectivity and control over reaction rates to avoid the formation of a wide range of undesired molecules. Some form of catalysis must have been incorporated in prebiotic systems at an early stage in order to direct reaction outcomes. Indeed, the RNA world scenario relies heavily upon the dual role of RNA as a catalyst as well as an information storage polymer. Furthermore, various transition metal ions and mineral surfaces have been widely used for their catalytic potential. However, with catalysts accelerating reactions, primordial systems would have risked rapid dissipation of high energy molecules. We are inspired by the way extant biology controls the flux of energy dissipation through the combination of kinetically stable and thermodynamically activated (KSTA) compounds, e.g. ATP, with enzyme catalysts, e.g. histidine kinases. Histidine kinases catalytic cycle proceeds via a phosphorylated histidyl residue in the active site (Figure ). The kinetic stability of KSTA compounds ensures that the chemical potential held within the molecule is not dissipated in deleterious side reactions. This is exemplified by the kinetic stability of ATP which has a hydrolysis half-life of 2 years at 25 °C and pH 8. This strategy of using KSTA compounds with enzyme catalysts is key to directing reaction outcomes in cellular biochemical networks.