Substrate attenuation: An approach to improve antibody catalysis

Kim D. Janda, Stephen J. Benkovic, Donald A. McLeod, Diane M. Schloeder, Richard A. Lerner

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Antibodies raised to quinaldine phosphonamide 1a showed no ability to hydrolyze its most homologous substrates amide and ester 2 and 3, respectively. However, within this same set of antibodies some thirteen showed a great propensity to hydrolyse a structurally similar naphthyl ester. In addition to heteroatom discrimination one of the antibodies examined in detail displayed an increase in catalytic efficiency presumably via weak apparent binding (Km) when phenylesters were employed as substrates. These findings suggest abzyme catalysis may be improved via substrate attenuation. Antibodies raised to quinaldine phosphonamide 1a showed no ability to hydrolyze its most homologous substrates amide and ester 2 and 3, respectively. However, within this same set of antibodies some thirteen showed a great propensity to hydrolyse a structurally similar naphthyl ester. In addition to heteroatom discrimination one of the antibodies examined in detail displayed an increase in catalytic efficiency presumably via weak apparent binding (Km) when phenylesters were employed as substrates. These findings suggest abzyme catalysis may be improved via substrate attenuation.

Original languageEnglish (US)
Pages (from-to)2503-2506
Number of pages4
JournalTetrahedron
Volume47
Issue number14-15
DOIs
StatePublished - 1991

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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