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An unexpectedly efficient catalytic antibody operating by ping-pong and induced fit mechanisms

Academic Article
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Overview

authors

  • Wirsching, P.
  • Ashley, J. A.
  • Benkovic, S. J.
  • Janda, Kim
  • Lerner, Richard

publication date

  • May 1991

journal

  • Science  Journal

abstract

  • A transition state analogue was used to produce a mouse antibody that catalyzes transesterification in water. The antibody behaves as a highly efficient catalyst with a covalent intermediate and the characteristic of induced fit. While some features of the catalytic pathway were programmed when the hapten was designed and reflect favorable substrate-antibody interactions, other features are a manifestation of the chemical potential of antibody diversity. The fact that antibodies recapitulate mechanisms and pathways previously thought to be a characteristic of highly evolved enzymes suggests that once an appropriate binding cavity is achieved, reaction pathways commensurate with the intrinsic chemical potential of proteins ensue.

subject areas

  • Acylation
  • Alcohols
  • Animals
  • Antibodies, Monoclonal
  • Antibody Specificity
  • Binding Sites, Antibody
  • Catalysis
  • Enzymes
  • Esterification
  • Haptens
  • Kinetics
  • Mice
  • Water
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2024120

PubMed ID

  • 2024120
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Additional Document Info

start page

  • 680

end page

  • 685

volume

  • 252

issue

  • 5006

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