We have shown that histidyl peptide catalysed phosphate transfer reactions could have plausibly been present at the origins of life. The use of histidyl peptide-based organocatalysts in our system provides an important link to the protein-based enzymes that life has adopted as the main type of catalyst for biochemical reactions. Notably, the formation of the phosphorylated histidyl intermediate in our experiments is reminiscent of the phosphorylated histidyl residues that are present in the catalytic cycle of histidine kinases (Figure ). Furthermore, the analogous catalytic cycle between our prebiotic histidyl peptides and histidine kinases is a link between this prebiotic chemistry and the biochemistry of life. We have shown that the histidyl peptides act as catalysts abiotically. But upon the advent of ribosomal peptide synthesis at the origins of life, we envision that these histidyl peptides could be subject to evolution in order to improve their catalytic activity for phosphorylation reactions and introduce substrate selectivity. Thus, our prebiotic system is primed to be taken over by life -once it emerges.