Antibody-catalyzed rearrangement of the peptide bond

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

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Abstract

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
JournalScience
Volume258
Issue number5083
DOIs
Publication statusPublished - Jan 1 1992

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All Science Journal Classification (ASJC) codes

  • General

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Gibbs, R. A., Taylor, S., & Benkovic, S. J. (1992). Antibody-catalyzed rearrangement of the peptide bond. Science, 258(5083), 803-805. https://doi.org/10.1126/science.1439788