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We reconstructed an ancestral nucleoside diphosphate kinase (NDK) scaffold using 10 prebiotically plausible residues plus lysine and arginine. The resulting variant, Arc1\u201012KR, retained the canonical NDK fold in its crystal structure despite lacking the catalytic histidine. Chromatographic and mass spectrometric analyses showed ADP disproportionation to ATP and AMP, an activity undetectable in the NDK scaffold prior to amino acid reduction. Kinetic analysis showed nonlinear dependence on ADP concentration, and docking\/molecular dynamics simulations indicated that the putative active\u2010site region can accommodate two ADP molecules. These structural, computational, and mutational analyses suggest that compositional constraints reshape ATP\u2010forming phosphoryl\u2010transfer chemistry through a reorganized active site in which aspartate and arginine, together with coordinated Mg\n                    <jats:sup>2+<\/jats:sup>\n                    , may enable phosphoryl transfer via a noncanonical, histidine\u2010independent mechanism. Despite modest catalytic efficiency, this activity represents a viable catalytic solution under compositional constraints, demonstrating that ATP formation can be supported by minimal amino acid repertoires. Thus, restricting amino acid diversity can generate distinct yet convergent ATP\u2010forming catalytic solutions, which may represent chemically plausible early routes to ATP formation under primitive conditions.\n                  <\/jats:p>","DOI":"10.1002\/anie.2166480","type":"journal-article","created":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T18:06:34Z","timestamp":1791569194000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Switching ATP\u2010Forming Phosphoryl\u2010Transfer Chemistry With a Restricted Set of Amino Acids"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7117-3318","authenticated-orcid":false,"given":"Sota","family":"Yagi","sequence":"first","affiliation":[{"name":"Faculty of Human Sciences Waseda University  Tokorozawa Saitama Japan"},{"name":"RIKEN Center for Integrative Medical Sciences  Yokohama Kanagawa 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