Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes

Science. 1995 Dec 15;270(5243):1797-800. doi: 10.1126/science.270.5243.1797.

Abstract

Antibodies that catalyze the aldol reaction, a basic carbon-carbon bond-forming reaction, have been generated. The mechanism for antibody catalysis of this reaction mimics that used by natural class I aldolase enzymes. Immunization with a reactive compound covalently trapped a Lys residue in the binding pocket of the antibody by formation of a stable vinylogous amide. The reaction mechanism for the formation of the covalent antibody-hapten complex was recruited to catalyze the aldol reaction. The antibodies use the epsilon-amino group of Lys to form an enamine with ketone substrates and use this enamine as a nascent carbon nucleophile to attack the second substrate, an aldehyde, to form a new carbon-carbon bond. The antibodies control the diastereofacial selectivity of the reaction in both Cram-Felkin and anti-Cram-Felkin directions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetone / chemistry
  • Aldehydes / chemistry
  • Animals
  • Antibodies, Catalytic / biosynthesis
  • Antibodies, Catalytic / chemistry*
  • Antibodies, Catalytic / immunology
  • Antibodies, Monoclonal / chemistry
  • Antibodies, Monoclonal / immunology
  • Antibody Specificity
  • Catalysis
  • Fructose-Bisphosphate Aldolase / chemistry*
  • Fructose-Bisphosphate Aldolase / immunology
  • Haptens / chemistry
  • Haptens / immunology
  • Lysine / chemistry
  • Mice
  • Substrate Specificity

Substances

  • Aldehydes
  • Antibodies, Catalytic
  • Antibodies, Monoclonal
  • Haptens
  • Acetone
  • Fructose-Bisphosphate Aldolase
  • Lysine