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An Unexpectedly Efficient Catalytic Antibody Operating by Ping-Pong and Induced Fit Mechanisms

Wirsching, Peter ; Ashley, Jon A. ; Benkovic, Stephen J. ; Janda, Kim D. ; Lerner, Richard A.

Science, 03 May 1991, Vol.252(5006), pp.680-685 [Periódico revisado por pares]

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  • Título:
    An Unexpectedly Efficient Catalytic Antibody Operating by Ping-Pong and Induced Fit Mechanisms
  • Autor: Wirsching, Peter ; Ashley, Jon A. ; Benkovic, Stephen J. ; Janda, Kim D. ; Lerner, Richard A.
  • Assuntos: Sciences (General) ; Biology
  • É parte de: Science, 03 May 1991, Vol.252(5006), pp.680-685
  • Descrição: 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.
  • Idioma: Inglês

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