A functional arginine residue in rabbit-muscle aldolase.
Rabbit muscle aldolase is irreversibly modified by the arginine-selective alpha-dicarbonyl, phenylglyoxal, loss of activity correlating with the unique modifications of one arginine residue per subunit, as determined by amino acid analysis, and (7-14C)phenylglyoxal incorporation. The affinity of the modified enzyme for dihydroxyacetone phosphate is significantly reduced while substantial protection against inactivation is afforded by fructose 1,6-disphosphate, dihydroxyacetone phosphate or phosphate ion. The nature of the substrate C-1 phosphate binding site in this enzyme is discussed in the light of these and other results.
D000818:Animals; D001120:Arginine / Q000032:analysis*; D001665:Binding Sites; D002074:Butanones / Q000494:pharmacology; D004099:Dihydroxyacetone Phosphate / Q000494:pharmacology; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005636:Fructosephosphates / Q000494:pharmacology; D006037:Glyoxal / Q000494:pharmacology; D006598:Hexosediphosphates / Q000494:pharmacology; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010710:Phosphates / Q000494:pharmacology; D011485:Protein Binding; D011817:Rabbits
D002074:Butanones; D005636:Fructosephosphates; D006598:Hexosediphosphates; D010710:Phosphates; D006037:Glyoxal; D004099:Dihydroxyacetone Phosphate; D001120:Arginine; D005634:Fructose-Bisphosphate Aldolase