1.4.1.13: glutamate synthase (NADPH)
This is an abbreviated version!
For detailed information about glutamate synthase (NADPH), go to the full flat file.
Word Map on EC 1.4.1.13
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1.4.1.13
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nitrate
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ammonia
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seedling
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no3
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ferredoxin-dependent
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chlorophyll
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shoot
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ferredoxin
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6.3.1.2
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iron-sulfur
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nadh-dependent
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azaserine
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nitrogenase
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1.4.7.1
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azospirillum
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assimilatory
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alpha-ketoglutarate
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brasilense
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amidotransferase
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glutaminase
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hydroponic
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photorespiratory
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photorespiration
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15n-labeled
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n2-fixing
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molecular biology
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nadp-glutamate
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heterocysts
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glutamine-dependent
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ureides
- 1.4.1.13
- nitrate
- ammonia
- seedling
- no3
-
ferredoxin-dependent
- chlorophyll
- shoot
- ferredoxin
-
6.3.1.2
-
iron-sulfur
-
nadh-dependent
- azaserine
- nitrogenase
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1.4.7.1
- azospirillum
-
assimilatory
- alpha-ketoglutarate
- brasilense
-
amidotransferase
- glutaminase
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hydroponic
-
photorespiratory
-
photorespiration
-
15n-labeled
-
n2-fixing
- molecular biology
-
nadp-glutamate
- heterocysts
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glutamine-dependent
-
ureides
Reaction
Synonyms
EC 2.6.1.53, EhNO1, EhNO2, gltA, gltB, GltB1, GltB2, gltD, GltS, glutamate synthetase (NADP), glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP), glutamine-ketoglutaric aminotransferase, GOGAT, L-glutamate synthase, L-glutamate synthetase, L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, NADPH-dependent glutamate synthase, NADPH-GltS, NADPH-glutamate synthase, NADPH-GOGAT, NADPH-linked glutamate synthase, pGLTY1, pGLTY2, pGLTZ, PH0876, PH1873, synthase, glutamate (reduced nicotinamide adenine dinucleotide phosphate)
ECTree
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Subunits
Subunits on EC 1.4.1.13 - glutamate synthase (NADPH)
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dimer
heterodimer
homodimer
2 * 200000, cryoelectron microscopy and small angle X-ray scattering
homohexamer
6 * 200000, cryoelectron microscopy and small angle X-ray scattering, the hexamer exhibits a concentration-dependent equilibrium with monomers and dimers, in solution the hexamer is destabilized by high ionic strength and to a lower extent by the reaction product NADP+
octamer
tetramer
additional information
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x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE
octamer
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4 * 53000 + 4 * 135000, SDS-PAGE, urea polyacrylamide gel electrophoresis
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gel filtration, aggregation state of NADPH-GltS alphabeta holoenzyme
analysis by synchrotron radiation x-ray solution scattering, alpha subunit and alphabeta holoenzyme are tetrameric in solution, beta subunit is a mixture of monomers and dimers. The (alphabeta)4 holoenzyme is similar to the tetrameric alpha4 complex with the beta subunits occupying the periphery, thus allowing independent catalytic activities of the alphabeta protomers
additional information
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analysis by synchrotron radiation x-ray solution scattering, alpha subunit and alphabeta holoenzyme are tetrameric in solution, beta subunit is a mixture of monomers and dimers. The (alphabeta)4 holoenzyme is similar to the tetrameric alpha4 complex with the beta subunits occupying the periphery, thus allowing independent catalytic activities of the alphabeta protomers
additional information
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modelling of unliganded alpha subunit as well as in complex with L-glutamine and 2-oxoglutarate, subunit exists in a catalytically inactive conformation unable to bind glutamine, and in a catalytically competent conformation, which is stabilized by the glutamine substrate. Binding of L-methionine sulfone causes a coordinated rigid-body motion that results in the inactive conformation