大肠杆菌对苏氨酸敏感的同型丝氨酸脱氢酶和天冬氨酸激酶活性

Paolo Truffa-Bachi, Gisèle Le Bras, Georges N. Cohen
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引用次数: 21

摘要

1.1. 在pH为9的Tris缓冲液中,对大肠杆菌的同型丝氨酸脱氢酶I (l-homoserine:NADP+ oxidoreductase, EC 1.1.1.3)进行了一级动力学灭活。这种失活伴随着酶对苏氨酸的脱敏。l -天冬氨酸和ATP,相关活性的底物,β-天冬氨酸激酶I (ATP: l -天冬氨酸4-磷酸转移酶,EC 2.7.2.4)保护抵抗同型丝氨酸脱氢酶的脱敏。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli

  • 1.

    1. Homoserine dehydrogenase I (l-homoserine:NADP+ oxidoreductase, EC 1.1.1.3) of Escherichia coli is inactivated with apparent first-order kinetics by exposure at pH 9 in Tris buffer. This inactivation is accompanied by desensitization of the enzyme towards threonine.

  • 2.

    2. L-Aspartate and ATP, the substrates of the associated activity, β-aspartokinase I (ATP:L-aspartate 4-phosphotransferase, EC 2.7.2.4) protect against the desensitization of homoserine dehydrogenase.

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