Enzymes of Nitrogen Metabolism in Legume Nodules: a Comparative Study

1978 ◽  
Vol 5 (5) ◽  
pp. 553 ◽  
Author(s):  
MJ Boland ◽  
HM Fordyce ◽  
RM Greenwood
Keyword(s):  
Glutamine Synthetase ◽  
Comparative Study ◽  
Glutamate Dehydrogenase ◽  
Nitrogen Metabolism ◽  
Glutamate Synthase ◽  
Ammonia Assimilation ◽  
Legume Species

Levels of activity of glutamine synthetase, glutamate dehydrogenase and NADH-dependent glutamate synthase in nodule cytoplasm extracts of twelve herbaceous legume species have been measured. Nodules of all species contained substantial quantities of glutamine synthetase. Levels of glutamate synthase were found to be between 7 and 100% of those of glutamine synthetase, while levels of glutamate dehydrogenase varied widely between 0.2 and 150% of those of glutamine synthetase. The estimated Km for hydroxylamine of glutamine synthetase was found to vary between 0.02 and 0.5 mM in nine species tested, while that of glutamate dehydrogenase for ammonia varied between 0.03 M and 0.1 M in the four species containing significant levels of that enzyme. It is proposed that the pathway of ammonia assimilation via glutamine synthetase and NADH-dependent glutamate synthase-catalysed reactions is universal in legume nodule metabolism.

Enzymes of ammonia assimilation in Rhizobium leguminosarum bacteroids

1975 ◽  
Vol 21 (7) ◽  
pp. 1009-1012 ◽  
Author(s):  
W. G. W. Kurz ◽  
D. A. Rokosh ◽  
T. A. Larue
Keyword(s):  
Glutamine Synthetase ◽  
Glutamate Dehydrogenase ◽  
Rhizobium Leguminosarum ◽  
Glutamate Synthase ◽  
Dinitrogen Fixation ◽  
Ammonia Assimilation ◽  
Enzymes Of Ammonia Assimilation

The activities of the following enzymes were studied in connection with dinitrogen fixation in pea bacteroids: glutamine synthetase (L-glutamate:ammonia ligase (ADP-forming)) (EC 6.3.1.2) (GS); glutamate dehydrogenase (NADP+) (L-glutamate:NADP+ oxidoreductase (deaminating)) (EC 1.4.1.4) (GDH); glutamate synthase (L-glutamine:2-oxoglutarate aminotransferase (NADPH-oxidizing)) (EC 2.6.1.53) (GOGAT). GS activity was high throughout the growth of the plant and GOGAT activity was always low. It is unlikely that GDH or the GS–GOGAT pathway can account for the incorporation of ammonia from dinitrogen fixation in the pea bacteroid.

Ammonia, glutamine, and asparagine: a carbon–nitrogen interface

1988 ◽  
Vol 66 (10) ◽  
pp. 2103-2109 ◽  
Author(s):  
K. W. Joy
Keyword(s):  
Glutamine Synthetase ◽  
Glutamate Dehydrogenase ◽  
Higher Plants ◽  
Amino Nitrogen ◽  
Glutamate Synthase ◽  
Dinitrogen Fixation ◽  
Similar Function ◽  
Metabolic Processes ◽  
Organic Form ◽  
Primary Input

In plants, the primary input of nitrogen (obtained from the soil or from symbiotic dinitrogen fixation) occurs through the assimilation of ammonia into organic form. Synthesis of glutamine (via glutamine synthetase) is the major, and possibly exclusive, route for this process, and there is little evidence for the participation of glutamate dehydrogenase. A variety of reactions distribute glutamine nitrogen to other compounds, including transfer to amino nitrogen through glutamate synthase. In many plants asparagine is a major recipient of glutamine nitrogen and provides a mobile reservoir for transport to sites of growth; ureides perform a similar function in some legumes. Utilisation of transport forms of nitrogen, and a number of other metabolic processes, involves release of ammonia, which must be reassimilated. In illuminated leaves, there is an extensive flux of ammonia released by the photorespiratory cycle, requiring continuous efficient reassimilation. Aspects of ammonia recycling and related amide metabolism in higher plants are reviewed.

Glutamate synthase levels in Neurospora crassa mutants altered with respect to nitrogen metabolism

1981 ◽  
Vol 1 (2) ◽  
pp. 158-164
Author(s):  
N S Dunn-Coleman ◽  
E A Robey ◽  
A B Tomsett ◽  
R H Garrett
Keyword(s):  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Nitrogen Metabolism ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Glutamate Synthase ◽  
Wild Type ◽  
Mutant Strains ◽  
Synthase Regulation ◽  
Glutamate Biosynthesis ◽  
Glutamine Limitation

Glutamate synthase catalyzes glutamate formation from 2-oxoglutarate plus glutamine and plays an essential role when glutamate biosynthesis by glutamate dehydrogenase is not possible. Glutamate synthase activity has been determined in a number of Neurospora crassa mutant strains with various defects in nitrogen metabolism. Of particular interest were two mutants phenotypically mute except in an am (biosynthetic nicotinamide adenine dinucleotide phosphate-glutamate dehydrogenase deficient, glutamate requiring) background. These mutants, i and en-am, are so-called enhancers of am; they have been redesignated herein as en(am)-1 and en(am)-2, respectively. Although glutamate synthase levels in en(am)-1 were essentially wild type, the en(am)-2 strain was devoid of glutamate synthase activity under all conditions examined, suggesting that en(am)-2 may be the structural locus for glutamate synthase. Regulation of glutamate synthase occurred to some extent, presumably in response to glutamate requirements. Glutamate starvation, as in am mutants, led to enhanced activity. In contrast, glutamine limitation, as in gln-1 mutants, depressed glutamate synthase levels.

Cellular and subcellular localisation of glutamine synthetase and glutamate dehydrogenase in grapes gives new insights on the regulation of carbon and nitrogen metabolism

Planta ◽  
2002 ◽  
Vol 216 (2) ◽  
pp. 245-254 ◽  
Author(s):  
Virginie Paczek ◽  
Fréréric Dubois ◽  
Rajbir Sangwan ◽  
Jean-François Morot-Gaudry ◽  
Kalliopi Roubelakis-Angelakis ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Glutamate Dehydrogenase ◽  
Nitrogen Metabolism ◽  
Subcellular Localisation ◽  
Carbon And Nitrogen ◽  
Carbon And Nitrogen Metabolism

scholarly journals Glutamate synthase levels in Neurospora crassa mutants altered with respect to nitrogen metabolism.

1981 ◽  
Vol 1 (2) ◽  
pp. 158-164 ◽  
Author(s):  
N S Dunn-Coleman ◽  
E A Robey ◽  
A B Tomsett ◽  
R H Garrett
Keyword(s):  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Nitrogen Metabolism ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Glutamate Synthase ◽  
Wild Type ◽  
Mutant Strains ◽  
Synthase Regulation ◽  
Glutamate Biosynthesis ◽  
Glutamine Limitation

Glutamate synthase catalyzes glutamate formation from 2-oxoglutarate plus glutamine and plays an essential role when glutamate biosynthesis by glutamate dehydrogenase is not possible. Glutamate synthase activity has been determined in a number of Neurospora crassa mutant strains with various defects in nitrogen metabolism. Of particular interest were two mutants phenotypically mute except in an am (biosynthetic nicotinamide adenine dinucleotide phosphate-glutamate dehydrogenase deficient, glutamate requiring) background. These mutants, i and en-am, are so-called enhancers of am; they have been redesignated herein as en(am)-1 and en(am)-2, respectively. Although glutamate synthase levels in en(am)-1 were essentially wild type, the en(am)-2 strain was devoid of glutamate synthase activity under all conditions examined, suggesting that en(am)-2 may be the structural locus for glutamate synthase. Regulation of glutamate synthase occurred to some extent, presumably in response to glutamate requirements. Glutamate starvation, as in am mutants, led to enhanced activity. In contrast, glutamine limitation, as in gln-1 mutants, depressed glutamate synthase levels.

scholarly journals Localization, Gene Expression, and Functions of Glutamine Synthetase Isozymes in Wheat Grain (Triticum aestivum L.)

2021 ◽  
Vol 12 ◽  
Author(s):  
Yihao Wei ◽  
Shuping Xiong ◽  
Zhiyong Zhang ◽  
Xiaodan Meng ◽  
Lulu Wang ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Metabolism ◽  
Glutamate Synthase ◽  
Grain Filling ◽  
Maximum Activity ◽  
Transfer Cells ◽  
Aleurone Layer ◽  
Wheat Grain ◽  
Plant Nitrogen ◽  
Endosperm Transfer Cells

Glutamine synthetase (GS) plays a major role in plant nitrogen metabolism, but the roles of individual GS isoforms in grains are unknown. Here, the localization and expression of individual TaGS isozymes in wheat grain were probed with TaGS isoenzyme-specific antibodies, and the nitrogen metabolism of grain during the grain filling stage were investigated. Immunofluorescence revealed that TaGS1;1, TaGS1;3, and TaGS2 were expressed in different regions of the embryo. In grain transporting tissues, TaGS1;2 was localized in vascular bundle; TaGS1;2 and TaGS1;1 were in chalaza and placentochalaza; TaGS1;1 and TaGS1;3 were in endosperm transfer cells; and TaGS1;3 and TaGS2 were in aleurone layer. GS exhibited maximum activity and expression at 8 days after flowering (DAF) with peak glutamine content in grains; from then, NH4+ increased largely from NO3- reduction, glutamate dehydrogenase (GDH) aminating activity increased continuously, and the activities of GS and glutamate synthase (GOGAT) decreased, while only TaGS1;3 kept a stable expression in different TaGS isozymes. Hence, GS-GOGAT cycle and GDH play different roles in NH4+ assimilation of grain in different stages of grain development; TaGS1;3, located in aleurone layer and endosperm transfer cells, plays a key role in Gln into endosperm for gluten synthesis. At 30 DAF, grain amino acids are mainly transported from maternal phloem.

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