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A Prebiotic Precursor to Life’s Phosphate Transfer System with an ATP Analog and Histidyl Peptide Organocatalysts
Biochemistry is dependent upon enzyme catalysts accelerating
key
reactions. At the origin of life, prebiotic chemistry must have incorporated
catalytic reactions. While this would have yielded much needed amplification
of certain reaction products, it would come at the possible cost of
rapidly depleting the high energy molecules that acted as chemical
fuels. Biochemistry solves this problem by combining kinetically stable
and thermodynamically activated molecules (e.g., ATP) with enzyme
catalysts. Here, we demonstrate a prebiotic phosphate transfer system
involving an ATP analog (imidazole phosphate) and histidyl peptides,
which function as organocatalytic enzyme analogs. We demonstrate that
histidyl peptides catalyze phosphorylations via a phosphorylated histidyl
intermediate. We integrate these histidyl-catalyzed phosphorylations
into a complete prebiotic scenario whereby inorganic phosphate is
incorporated into organic compounds though physicochemical wet–dry
cycles. Our work demonstrates a plausible system for the catalyzed
production of phosphorylated compounds on the early Earth and how
organocatalytic peptides, as enzyme precursors, could have played
an important role in this