X-ray structures of two families of hydrolytic antibodies

Benôt Gigant, Jean Baptiste Charbonnier, Beatrice Golinelli-Pimpaneau, Z. Eshhar, Bernard S. Green, Marcel Knossow*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The catalytic mechanisms of two esterase-like catalytic antibodies (Abs) have been determined, based on kinetic data and on structures of the complexes with transition-state analogs and with a stable substrate analog of the reactions they catalyze. Both Abs stabilize the oxyanion intermediate close to the transition state in ester hydrolysis. The different geometries of the hydrogen bonds that participate in this stabilization account for most of the difference between the efficiencies of these two Abs.

Original languageEnglish
Pages (from-to)25-32
Number of pages8
JournalApplied Biochemistry and Biotechnology
Volume75
Issue number1
DOIs
StatePublished - 1998

Keywords

  • Catalysis
  • Catalytic antibody
  • Ester hydrolysis
  • Oxyanion hole
  • Phosphonate hapten

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