Antibody-catalyzed rearrangement of the peptide bond

Richard A. Gibbs, Scott Taylor, Stephen J. Benkovic

Research output: Contribution to journalArticle

40 Scopus citations


The generation of antibodies from a bifunctional cyclic phosphinate transition-state analog provided agents capable of efficiently catalyzing both steps of the overall conversion of a substrate containing an asparaginyl-glycyl sequence through a succinimide intermediate to the products aspartyl-glycyl and the rearranged isoaspartyl-glycyl sequence. This reaction provides a potential means in addition to amide cleavage for the deactivation of protein or peptide biological functions in vivo.

Original languageEnglish (US)
Pages (from-to)803-805
Number of pages3
Issue number5083
Publication statusPublished - Jan 1 1992


All Science Journal Classification (ASJC) codes

  • General

Cite this

Gibbs, R. A., Taylor, S., & Benkovic, S. J. (1992). Antibody-catalyzed rearrangement of the peptide bond. Science, 258(5083), 803-805.