Antibody-catalyzed rearrangement of the peptide bond

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

Antibody-catalyzed rearrangement of the peptide bond

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

Chemistry

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

45 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
State	Published - Oct 30 1992

All Science Journal Classification (ASJC) codes

General

Cite this

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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.\}",

year = "1992",

month = oct,

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language = "English (US)",

volume = "258",

pages = "803--805",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "5083",

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TY - JOUR

T1 - Antibody-catalyzed rearrangement of the peptide bond

AU - Gibbs, Richard A.

AU - Taylor, Scott

AU - Benkovic, Stephen J.

PY - 1992/10/30

Y1 - 1992/10/30

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.

UR - https://www.scopus.com/pages/publications/0027129567

UR - https://www.scopus.com/pages/publications/0027129567#tab=citedBy

M3 - Article

C2 - 1439788

AN - SCOPUS:0027129567

SN - 0036-8075

VL - 258

SP - 803

EP - 805

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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