Biology Department, University College London, Gower Street, London WC1E6BT.
Plant Physiol. 1991 Feb;95(2):509-16. doi: 10.1104/pp.95.2.509.
In vivo nuclear magnetic resonance spectroscopy, in vitro gas chromatography-mass spectrometry, and automated (15)N/(13)C mass spectrometry have been used to demonstrate that glutamate dehydrogenase is active in the oxidation of glutamate, but not in the reductive amination of 2-oxogiutarate. In cell suspension cultures of carrot (Daucus carota L. cv Chantenay), primary assimilation of ammonium occurs via the glutamate synthase pathway. Glutamate dehydrogenase is derepressed in carbonlimited cells and in such cells the function of glutamate dehydrogenase appears to be the oxidation of glutamate, thus ensuring sufficient carbon skeletons for effective functioning of the tricarboxylic acid cycle. This catabolic role for glutamate dehydrogenase implies an important regulatory function in carbon and nitrogen metabolism.
体内磁共振波谱分析、体外气相色谱-质谱分析和自动化 (15)N/(13)C 质谱分析已经证明谷氨酸脱氢酶在谷氨酸的氧化中是活跃的,但在 2-酮戊二酸的还原胺化中不是活跃的。在胡萝卜(Daucus carota L. cv Chantenay)的细胞悬浮培养物中,铵的最初同化是通过谷氨酸合酶途径进行的。在碳限制的细胞中,谷氨酸脱氢酶被去阻遏,在这些细胞中,谷氨酸脱氢酶的功能似乎是谷氨酸的氧化,从而确保了足够的碳骨架,以有效地发挥三羧酸循环的作用。谷氨酸脱氢酶的这种分解代谢作用意味着它在碳氮代谢中具有重要的调节功能。