A Completely de Novo ATPase from Combinatorial Protein Design

Michael S. Wang, Michael H. Hecht

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Our understanding of biological chemistry is shaped by the observation that all life comes from other life - as Pasteur put it, omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancestry. Here we describe an enzyme designed completely de novo that hydrolyzes ATP. This protein was designed to lack β-sheet structure and is competitively inhibited by magnesium, two traits that are unlike natural ATPases.

Original languageEnglish (US)
Pages (from-to)15230-15234
Number of pages5
JournalJournal of the American Chemical Society
Issue number36
StatePublished - Sep 9 2020

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Biochemistry
  • Catalysis
  • Colloid and Surface Chemistry


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