While catalytic antibodies are well established as artificial catalysts with enzyme-like properties for a variety of reactions,1 few amidase antibodies have been obtained so far.2 Recently, we have described the preparation and kinetic characterization of amidase antibody 312d6.3 The antibody was raised against the sulfonamide hapten 2 a, designed to induce catalysis by transition-state mimicry and torsional activation, and has been found to accelerate the hydrolysis of amides 3 a, 4 a by a factor of 103 Here we report the results of a docking analysis carried out on the homology model of the variable fragment (Fv) region of antibody 312d6. A novel catalytic motif based on an arginine dyad, unprecedented in antibody hydrolases, is identified by this study.

An unprecedented catalytic motif revealed in the model structure of amide hydrolyzing antibody 312d6

PUCILLO, Carlo Ennio Michele;
2004-01-01

Abstract

While catalytic antibodies are well established as artificial catalysts with enzyme-like properties for a variety of reactions,1 few amidase antibodies have been obtained so far.2 Recently, we have described the preparation and kinetic characterization of amidase antibody 312d6.3 The antibody was raised against the sulfonamide hapten 2 a, designed to induce catalysis by transition-state mimicry and torsional activation, and has been found to accelerate the hydrolysis of amides 3 a, 4 a by a factor of 103 Here we report the results of a docking analysis carried out on the homology model of the variable fragment (Fv) region of antibody 312d6. A novel catalytic motif based on an arginine dyad, unprecedented in antibody hydrolases, is identified by this study.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11390/859208
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