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Glutamate in plants: metabolism, regulation and signalling

Forde, Brian and Lea, Peter (2007) Glutamate in plants: metabolism, regulation and signalling. Journal of Experimental Botany, 58 (9). pp. 2339-2358. ISSN 1460-2431

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Abstract

Glutamate occupies a central position in amino acid metabolism in plants. The acidic amino acid is formed by the action of glutamate synthase, utilizing glutamine and 2-oxoglutarate. However, glutamate is also the substrate for the synthesis of glutamine from ammonia, catalysed by glutamine synthetase. The a-amino group of glutamate may be transferred to other amino acids by the action of a wide range of multispecific aminotransferases. In addition, both the carbon skeleton and a-amino group of glutamate form the basis for the synthesis of g-aminobutyric acid, arginine, and proline. Finally, glutamate may be deaminated by glutamate dehydrogenase to form ammonia and 2-oxoglutarate. The possibility that the cellular concentrations of glutamate within the plant are homeostatically regulated by the combined action of these pathways is examined. Evidence that the well known signalling properties of glutamate in animals may also extend to the plant kingdom is reviewed. The existence in plants of glutamate-activated ion channels and their possible relationship to the GLR gene family that is homologous to ionotropic glutamate receptors (iGluRs) in animals are discussed. Glutamate signalling is examined from an evolutionary perspective, and the roles it might play in plants, both in endogenous signalling pathways and in determining the capacity of the root to respond to sources of organic N in the soil, are considered.

Item Type: Article
Journal or Publication Title: Journal of Experimental Botany
Uncontrolled Keywords: glutamate ; SIGNALING ; Metabolism ; glutamate receptor
Subjects:
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 53626
Deposited By: ep_importer_pure
Deposited On: 20 Apr 2012 16:27
Refereed?: Yes
Published?: Published
Last Modified: 09 Apr 2014 23:20
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/53626

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