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Literature summary for 1.4.1.2 extracted from

  • Labboun, S.; Terce-Laforgue, T.; Roscher, A.; Bedu, M.; Restivo, F.M.; Velanis, C.N.; Skopelitis, D.S.; Moshou, P.N.; Roubelakis-Angelakis, K.A.; Suzuki, A.; Hirel, B.
    Resolving the role of plant glutamate dehydrogenase. I. In vivo real time nuclear magnetic resonance spectroscopy experiments (2009), Plant Cell Physiol., 50, 1761-1773.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
molecular biology GDH, in conjunction with NADH-glutamte synthase, contributes to the control of leaf glutamate homeostasis, an amino acid that plays a central signaling and metabolic role at the interface of the carbon and nitrogen assimilatory pathways Nicotiana tabacum

Organism

Organism UniProt Comment Textmining
Nicotiana tabacum
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Source Tissue

Source Tissue Comment Organism Textmining
leaf
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 Nicotiana tabacum
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Synonyms

Synonyms Comment Organism
GDH
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 Nicotiana tabacum
glutamate dehydrogenase
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 Nicotiana tabacum

General Information

General Information Comment Organism
physiological function transgenic tobacco plants overexpressing the two genes encoding the enzyme are generated. Using an in vivo real time 15 N-nuclear magnetic resonance (NMR) spectroscopy approach it is shown that, when the two GDH genes are overexpressed individually or simultaneously, the transgenic plant leaves do not synthesize glutamate in the presence of NH4+ when glutamine synthetase is inhibited. When the two GDH unlabeled substrates ammonium and glutamate are provided simultaneously with either (15N) glutamate or 15NH4+ respectively, it is found that the ammonium released from the deamination of glutamate is reassimilated by the enzyme glutamine synthase, suggesting the occurrence of a futile cycle recycling both ammonium and glutamate Nicotiana tabacum