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THE ROLE OF AMMONIA ASSIMILATORY ENZYMES DURING NITROGEN FIXATION IN ROOT NODULES

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In legume root nodules over 95% of the nitrogen fixed by the bacteroid is excreted into the host plant as ammonia. Tracer (both 13N and 15N), enzyme and inhibitor studies all suggest that this ammonia is initially assimilated into the amide position of glutamine by the enzyme glutamine synthetase (GS) and then into the 2-amino position of glutamate by glutamate synthase. These two enzymes constitute the glutamate synthase cycle and are important as they catalyse the fust steps of N metabolism in the plant during nitrogen fixation. In this review the properties, localisation and regulation of GS and glutamate synthase are discussed. In temperate legumes (e.g. Pisum and Vicia), glutamate amino-N and glutamine amido-N are used directly to synthesize the major N transport compound asparagine. In tropical legumes, however (e.g. Glycine and Vigna), ureides are the predominant N compound transported to the shoot and are formed either directly from glutamine amido-N or via aspartate and glycine. Recent developments in the elucidation of this pathway are described and a comparison of the energy cost of ureide and asparagine synthesis and transport made. Glutamate dehydrogenase (GDH) located both in the bacteroid and in the plant mitochondrial fraction of the nodule does not appear to play any role in ammonia assimilation in legumes although evidence that it may function in Alnus nodules is discussed.

Affiliations: 1: Biochemistry Department, Rothamsted Experimental Station ; 2: I. A. R. & T., University of Ife

10.1080/0021213X.1982.10676938
/content/journals/10.1080/0021213x.1982.10676938
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/content/journals/10.1080/0021213x.1982.10676938
1982-05-13
2018-06-19

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