Chemical Bypass of Intein‐Catalyzed N–S Acyl Shift in Protein Splicing

Abstract

Spliced: An N-methyl group was introduced at the scissile peptide bond in a semisynthetic intein precursor. With the chemical modification, thioester formation and protein splicing was observed in the absence of the otherwise critical block B histidine. This finding shows the role of the histidine in ground-state destabilization and rules out other previously proposed roles for this residue in the protein splicing pathway. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.