EC Number   |
General Information |
Reference |
|---|
    1.4.1.14 | malfunction |
enzyme disruption in Oidiodendron maius induces reorganization of the N pathway and reduces tolerance to heavy-metals like zinc |
742607 |
| 1.4.1.14 | physiological function |
isoform NADH-GOGAT1 is important in the primary assimilation of NH4+ taken up by rice roots, while isoform NADH-GOGAT2 is important in remobilization of nitrogen during natural senescence |
742994 |
| 1.4.1.14 | physiological function |
NADH-dependent glutamate synthase plays a key role in assimilating ammonium in the Arabidopsis root |
743425 |
| 1.4.1.14 | physiological function |
NADH-GOGAT1 insertion mutants show significant reduction in NADH-GOGAT activity in the grain. The grain weight of neither the NADH-GOGAT1 mutant nor that of the NADH-GOGAT2 mutant is significantly different from that of Nipponbare. The NADH-GOGAT1 mutant does not show a significant difference in grain protein concentration. Loss-of-function of NADH-GOGAT1 leads to an increase in glutelin acidic (14%) and basic subunits (19%). Both the NADH-GOGAT1 and the NADH-GOGAT2 mutant show higher free amino acid concentrations in their grains than does Nipponbare |
763311 |
| 1.4.1.14 | physiological function |
the glutamine synthetase-glutamate synthase cycle plays an important role for proline synthesis in tomato leaves during salinity stress, while NADH-dependent glutamate synthase (NADHGOGAT) activity is unchanged due to salinity stress |
-, 725140 |
| 1.4.1.14 | physiological function |
the grain weight of neither the NADH-GOGAT1 mutant nor that of the NADH-GOGAT2 mutant is significantly different from that of Nipponbare. A loss of NADH-GOGAT2 function leads to an increase of almost 20% in grain protein concentration. Loss-of-function of NADH-GOGAT2 leads to an increase in concentrations of both glutelins and prolamins. The concentrations of all glutelins, their precursors, and their acidic and basic subunits in the NADH-GOGAT2 mutant increases by 27-40%. Prolamins accumulate in the grains of the NADH-GOGAT2 mutant to higher concentrations. Both the NADH-GOGAT1 and the NADH-GOGAT2 mutant show higher free amino acid concentrations in their grains than does Nipponbare |
763311 |
