Antibody-Catalyzed Rearrangement of the Peptide Bond
- 30 October 1992
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 258 (5083) , 803-805
- https://doi.org/10.1126/science.1439788
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.Keywords
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