Plant Physiology 95:509-516 (1991)
© 1991 American Society of Plant Biologists
Metabolism and Enzymology
The Role of Glutamate Dehydrogenase in Plant Nitrogen Metabolism 1,2
Sharon A. Robinson,
Annette P. Slade,
Gary G. Fox,
Richard Phillips,
R. George Ratcliffe and
George R. Stewart
Biology Department, University College London, Gower Street, London WC1E6BT,
Department of Plant Sciences, Oxford University, Agricultural Science Building, Parks Road, Oxford OX1 3PF
In vivo nuclear magnetic resonance spectroscopy, in vitro gas chromatography-mass spectrometry, and automated 15N/13C 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.
1 S. A. R. and A. P. S. were supported the Science and Engineering Research Council. G. G. F. was supported by a Science and Engineering Council CASE studentship with Unilever Research. R. G. R. acknowledges the financial support of the Agricultural and Food Research Council.
2 This paper is dedicated to the memory of Dr. A. P. Sims who initiated the use of 15N isotopes in studies of plant nitrogen metabolism.
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