Specific inhibition of aspartase by S-2,3-dicarboxyaziridine.
Aspartase of Escherichia coli was inhibited in a competitive manner by S-2,3-dicarboxyazirdine (DCAZ), an antibacterial substance against Aeromonas salmonesida. The inhibition constant (Ki) was 55 microM, which was as low as less than one tenth that of the Km value for the substrate, L-aspartate. In view of the fact that both aspartase and fumarase (J. Greenhut et al. (1985) J. Biol. Chem. 260, 6684-6686) were inhibited by DCAZ in competitive manners, common features of the reaction mechanism of the two enzymes were discussed.
Higashi
Y
Y
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
Tokushige
M
M
Umezawa
H
H
D000642:Ammonia-Lyases / Q000037:antagonists & inhibitors*; D001220:Aspartate Ammonia-Lyase / Q000037:antagonists & inhibitors*; D001388:Aziridines / Q000494:pharmacology*; D001389:Azirines / Q000494:pharmacology*; D001667:Binding, Competitive; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics
D001388:Aziridines; D001389:Azirines; C045613:2,3-dicarboxyaziridine; D000642:Ammonia-Lyases; D001220:Aspartate Ammonia-Lyase