An enzyme catalyst for phosphate transfer is clearly not compatible with prebiotic chemistry. However, peptides on the early Earth are considered to be plausible prebiotic organocatalysts. Histidyl-based peptides have shown promise as prebiotic organocatalysts. His-His can catalyse the oligomerisation of peptides, the dephosphorylation of nucleotides, the hydrolysis of oligonucleotides and the oligomerisation reaction with c2,3-nucleotides. His-His is proposed to derive its catalytic activity from a general acid-base catalysis by proton relay mechanism. Ser-His is another prebiotic organocatalyst that catalyses a wide range of reactions e.g. peptide bond formation between an amino acid ester and an amino acid. This was exploited to drive vesicle growth via Ser-His localising inside the membrane of vesicles and catalysing the formation of a hydrophobic dipeptide. Ser-His can catalyse the formation of oligonucleotides starting from imidazole-activated nucleotides. Histidyl containing cyclic peptides catalyse also the hydrolysis of pyrophosphate. Histidine may also ligate metals e.g. Zn to form complexes that catalyse depsipeptide oligomerisation. In our aforementioned physicochemical orthophosphate cycle, we hypothesized that a histidyl peptide could serve as a catalyst for Figure . a) The phosphate transfer system used by life with ATP as a kinetically stable and thermodynamically activated source of phosphate and enzymes, such as histidine kinases, which catalyse phosphorylation reactions to a nucleophilic biomolecule (R-OH). b) The prebiotic phosphate transfer system demonstrated here with imidazole phosphate as a kinetically stable and thermodynamically activated phosphate source and a histidyl peptide as a prebiotic organocatalyst for the phosphorylation of organic building blocks of life (R-OH).