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Antibody-catalyzed rearrangement of the peptide bond
R A Gibbs1, S Taylor, S J Benkovic
1Department of Chemistry, Pennsylvania State University, University Park 16802.
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.
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