STUDIES ON THE INTERACTION OF FRUCTOSE 1,6-P2 ALDOLASE WITH METHYLGLYOXAL

  • 1 January 1980
    • journal article
    • research article
    • Vol. 29  (4) , 289-299
Abstract
Reaction of rabbit muscle fructose 1,6-bisphosphate aldolase with methylglyoxal results in a biphasic loss of activity. The kinetics of the initial rapid phase are 1st-order with respect to the inhibitor. Dihydroxyacetone phosphate [DHAP] and fructose 1,6-bisphosphate afford complete protection, whereas Pi provides only partial protection against inactivation. The treatment with methylglyoxal modifies the aldolase ability to bind D-Ga3P [D-glyceraldahyde-3 phosphate] and DHAP. Loss of activity correlates with the modification of 1.7 arginine residues, but data suggest that probably 1 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.

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