1.4.1.14: glutamate synthase (NADH)
This is an abbreviated version!
For detailed information about glutamate synthase (NADH), go to the full flat file.
Reaction
Synonyms
gltA, GltA2, gltB, glutamate (reduced nicotinamide adenine dinucleotide) synthase, glutamate synthase, glutamate synthase (NADH), glutamate synthase (NADH-dependent), glutamate synthetase, glutamine 2-oxoglutarate aminotransferase, GOGAT, GOGAT1, GOGAT2, L-glutamate synthase (NADH), L-glutamate synthetase, NADH glutamate synthase, NADH-dependent glutamate synthase, NADH-dependent glutamine-2-oxoglutarate aminotransferase, NADH-GltS, NADH-glutamate synthase, NADH-GOGAT, NADH-GOGAT I, NADH-GOGAT II, NADH-GOGAT1, NADH-GOGAT2, NADH: GOGAT, Os01g0681900, Os05g0555600, synthase, glutamate (reduced nicotinamide adenine dinucleotide)
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General Information
General Information on EC 1.4.1.14 - glutamate synthase (NADH)
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malfunction
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enzyme disruption in Oidiodendron maius induces reorganization of the N pathway and reduces tolerance to heavy-metals like zinc
physiological function
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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
physiological function
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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
physiological function
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NADH-dependent glutamate synthase plays a key role in assimilating ammonium in the Arabidopsis root
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
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
physiological function
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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
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