Antibody-catalyzed rearrangement of the peptide bond

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

doi:10.1126/science.1439788

Antibody-catalyzed rearrangement of the peptide bond

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

Chemistry

Research output: Contribution to journal › Article › peer-review

42 Scopus citations

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 language	English (US)
Pages (from-to)	803-805
Number of pages	3
Journal	Science
Volume	258
Issue number	5083
DOIs	https://doi.org/10.1126/science.1439788
State	Published - 1992

All Science Journal Classification (ASJC) codes

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title = "Antibody-catalyzed rearrangement of the peptide bond",

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.",

author = "Gibbs, {Richard A.} and Scott Taylor and Benkovic, {Stephen J.}",

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T1 - Antibody-catalyzed rearrangement of the peptide bond

AU - Gibbs, Richard A.

AU - Taylor, Scott

AU - Benkovic, Stephen J.

PY - 1992

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N2 - 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.

AB - 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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DO - 10.1126/science.1439788

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SP - 803

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JO - Science

JF - Science

IS - 5083

ER -

Antibody-catalyzed rearrangement of the peptide bond

Abstract

All Science Journal Classification (ASJC) codes

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