Fumaraldehydic acid-induced inactivation of aspartase.
Fumaraldehydic acid (FAA) induced a time-dependent inactivation of aspartase (L-aspartate ammonia-lyase, EC 4.3.1.1) from Escherichia coli at 30 degrees C and pH 7.4 following pseudo-first order kinetics. The rate of inactivation increased in proportion to the FAA concentration. In addition, the rate of inactivation increased, as the pH was increased. Determination of sulfhydryl groups showed that approximately one among 11 sulfhydryl groups was modified by FAA concomitant with the inactivation. L-Aspartate and fumarate protected the enzyme against FAA-inactivation, when Mg2+ ions were present. Unlike E. coli aspartase, P. fluorescens aspartase was not inactivated by FAA.
D000642:Ammonia-Lyases / Q000037:antagonists & inhibitors*; D001220:Aspartate Ammonia-Lyase / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology; D005229:Fatty Acids, Monounsaturated / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011551:Pseudomonas fluorescens / Q000201:enzymology; D013438:Sulfhydryl Compounds / Q000032:analysis
D005229:Fatty Acids, Monounsaturated; D013438:Sulfhydryl Compounds; C057684:fumaraldehydic acid; D000642:Ammonia-Lyases; D001220:Aspartate Ammonia-Lyase