Plant Physiology 98:1190-1195 (1992)
© 1992 American Society of Plant Biologists
Metabolism and Enzymology
Regulation of Glutamate Dehydrogenase Activity in Relation to Carbon Limitation and Protein Catabolism in Carrot Cell Suspension Cultures 1
Sharon A. Robinson2,
George R. Stewart3 and
Richard Phillips
Department of Biology, Darwin Building, University College London, Gower Street, London WC1E 6BT, England
Glutamate dehydrogenase (GDH) specific activity and function have been studied in cell suspension cultures of carrot (Daucus carota L. cv Chantenay) in response to carbon and nitrogen supply in the culture medium. The specific activity of GDH was derepressed in sucrose-starved cells concomitant with protein catabolism, ammonium excretion, and the accumulation of metabolically active amino acids. The addition of sucrose led to a rapid decrease in GDH specific activity, an uptake of ammonium from the medium, and a decrease in amino acid levels. The extent of GDH derepression was correlated positively with cellular glutamate concentration. These findings strengthen the view that the function of GDH is the catabolism of glutamate, which under conditions of carbon stress provides carbon skeletons for tricarboxylic acid cycle activity.
2 Present address: Director's Unit, Research School of Biological Sciences, The Australian National University, Box 475, Canberra 2601, Australia.
3 Present address: Department of Botany, The University of Queensland, St. Lucia, Brisbane, Australia.
1 S.A.R. was supported by the Science and Engineering Research Council.
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