We sought a prebiotically plausible catalyst to overcome the kinetic stability of imidazole phosphate and thereby control the release of the energy in the phosphate transfer reaction. We noted that in extant life histidine kinases catalyse phosphorylation reactions. We reasoned that histidine/histidyl residue could be a plausible prebiotic organocatalyst to overcome the kinetic stability of imidazole phosphate due to the structural similarity between imidazole and the imidazolyl ring on histidine. Prebiotic syntheses of histidine and histidyl residue containing peptides are known. In our previous study on the formation of imidazole phosphate, we observed that in water imidazole phosphate slowly hydrolysed over time. Therefore to test whether histidyl peptides act as catalysts for phosphate transfer we chose to study the hydrolysis of imidazole phosphate.