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

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

Research output: Contribution to journalArticle

89 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)680-685
Number of pages6
JournalScience
Volume252
Issue number5006
DOIs
StatePublished - Jan 1 1991

All Science Journal Classification (ASJC) codes

  • General

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    Wirsching, P., Ashley, J. A., Benkovic, S. J., Janda, K. D., & Lerner, R. A. (1991). An unexpectedly efficient catalytic antibody operating by ping-pong and induced fit mechanisms. Science, 252(5006), 680-685. https://doi.org/10.1126/science.2024120