All of our chemistry functions under the most benign of conditions at pH 7.3 -7.5 and 22 °C. Unlike most other prebiotic methods for phosphate transfer, no heating or other aggressive physical or chemical conditions are required. Our chemistry makes use of wet-dry cycles in order to enable the phosphorylation of organic compounds in a paste. Such wetdry cycles are commonly exploited in prebiotic chemistry. Whilst it would be ideal for this chemistry to function ultimately without the need for a wet-dry cycle, we note that life also does not perform phosphorylation reactions in solution but rather inside enzyme active sites. Active sites have a different physical environment to that of bulk solution. A common feature of many enzymes is the dissolution of substrates upon entering the active site and expulsion of water molecules already present in the active site. Consequently, the activity of water within the active site is lower than in bulk solution. In our experiments the phosphorylation of organic compounds only takes place in water-depleted pastes not in solution due to the lower activity of water in the paste. In addition, our use of histidyl peptides opens a conceivable pathway for formation of an enzyme-like active site. Elongation of the histidyl peptide chain could enable the formation of a tertiary structure with an active site which excludes water and thus has a lower water activity. Additionally, wet-dry cycles provide a mean of environmental control over when reactions occur. These and other such environmental cycles could have imprinted periodic patterns on prebiotic chemistry that may have been harnessed by the earliest chemical reaction networks. In conclusion, we have demonstrated here a prebiotic precursor to Life's phosphate transfer system with imidazole phosphate as an ATP analogue and histidyl peptide catalysts as kinase enzyme analogues. Our system demonstrates a new organocatalytic-role for peptides with histidyl residues at the origins of life. This system is constructed according to the same chemical strategy that life uses with kinetically stable and thermodynamically activated molecules with peptide/protein-catalysts. Thus, our work presents an important step forward in the advance of prebiotic chemical reaction networks towards life.