Studies on the interaction of fructose 1,6-P2 aldolase with methylglyoxal.

Reaction of rabbit muscle fructose 1,6-P2 aldolase with methylglyoxal results in a biphasic loss of activity. The kinetics of the initial rapid phase are first order with respect to the inhibitor. Dihydroxyacetone phosphate and fructose 1,6 bisphosphate afford complete protection whereas inorganic phosphate provides only a partial protection against inactivation. The treatment with methylglyoxal modifies the aldolase ability to bind D-Ga3P and DHAP. Loss of activity correlates with the modification of 1.7 arginine residues but data suggest that probably one of these arginine residues is essential. A likely role of this residue could be its interaction with the C1 negatively charged phosphate binding site of the enzyme.