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X-Ray structures of two families of hydrolytic antibodies |
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| Authors: | Benoît Gigant Jean-Baptiste Charbonnier Beatrice Golinelli-Pimpaneau Z Eshhar Bernard S Green Marcel Knossow |
| Institution: | (1) Laboratoire d’Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Bat. 34, Avenue de la Terrasse, 91198 Gif sur Yvette Cedex, France;(2) Department of Immunology, The Weizmann Institute of Science, Rehovot, Israel;(3) Department of Pharmaceutical Chemistry, The Hebrew University School of Pharmacy, Jerusalem, Israel |
| 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. |
| Keywords: | Phosphonate hapten ester hydrolysis oxyanion hole catalytic antibody catalysis |
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