Debashrito Deb

Abstract In biological systems, adenosine triphosphate (ATP) provides an energetic driving force for peptide bond formation, but protein chemists lack tools that emulate this strategy. Here we develop an ATP-driven platform for C-terminal activation and peptide ligation based on MccB, a bacterial ancestor of ubiquitin-activating (E1) enzymes.

Abstract In biological systems, ATP provides an energetic driving force for peptide bond formation, but protein chemists lack tools that emulate this strategy. Inspired by the eukaryotic ubiquitination cascade, we developed an ATP-driven platform for C-terminal activation and peptide ligation based on E. coli MccB, a bacterial ancestor of ubiquitin-activating (E1) enzymes that natively catalyzes C-terminal phosphoramidate bond formation.