Higashi Y, Tokushige M, Umezawa H
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
Biochem Int. 1988 Mar;16(3):449-52.
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.
大肠杆菌天冬氨酸酶受到S-2,3-二羧基氮丙啶（DCAZ，一种抗鲑鱼气单胞菌的抗菌物质）的竞争性抑制。抑制常数（Ki）为55微摩尔，低至底物L-天冬氨酸Km值的十分之一以下。鉴于天冬氨酸酶和延胡索酸酶（J. Greenhut等人（1985年）《生物化学杂志》260, 6684-6686）均受到DCAZ的竞争性抑制，讨论了这两种酶反应机制的共同特征。
