Irreversible inhibition of aldolase by a phosphorylated alpha-dicarbonyl compound |
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Authors: | Chabot Nicolas Vinatier Virginie Gefflaut Thierry Baudoin Cecile Rodriguez Frederic Blonski Casimir Hoffmann Pascal |
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Affiliation: | Groupe de Chimie Organique Biologique, Laboratoire LSPCMIB - UMR 5068 CNRS, Université Paul Sabatier, Toulouse cedex 9, France. |
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Abstract: | The preparation of a phosphorylated alpha-dicarbonyl compound designed to specifically react with arginine residues of enzymes accepting phosphorylated compounds as effectors is reported, and shown to inhibit rabbit muscle aldolase in a time-dependent and irreversible manner. This irreversible inhibition occured in a buffer devoid of borate ions, suggesting that the presence of the phosphate moiety contributes in the stabilization of the adduct formed with arginine residues. Under the same conditions, the metalloenzyme iron superoxide dismutase, in which an arginine is known to be critical for the catalytic function, is not significantly inhibited. |
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