Antibody-catalyzed rearrangement of the peptide bond

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Science  30 Oct 1992:
Vol. 258, Issue 5083, pp. 803-805
DOI: 10.1126/science.1439788


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.