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Science 30 October 1992:
Vol. 258. no. 5083, pp. 803 - 805
DOI: 10.1126/science.1439788
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Articles

Science, Vol 258, Issue 5083, 803-805
Copyright © 1992 by American Association for the Advancement of Science

articles

Antibody-catalyzed rearrangement of the peptide bond

RA Gibbs, S Taylor, and SJ Benkovic

Department of Chemistry, Pennsylvania State University, University Park 16802.

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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Science. ISSN 0036-8075 (print), 1095-9203 (online)