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
-
hydroponic
-
photorespiratory
-
photorespiration
-
15n-labeled
-
n2-fixing
- molecular biology
-
nadp-glutamate
- heterocysts
-
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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KM Value
KM Value on EC 1.4.1.13 - glutamate synthase (NADPH)
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0.017
acetylpyridine-NADPH
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in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 3.7% that obtained in the presence of NADPH
0.14
ferricyanide
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of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.05
iodonitrotetrazolium
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of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.035
menadione
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of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.01
thio-NADPH
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in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 54% that obtained in the presence of NADPH
0.23
2-oxoglutarate
dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 0.1 mM NADPH
0.24
2-oxoglutarate
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NH3-dependent glutamate synthase and apoglutamate synthase
0.75
2-oxoglutarate
hexameric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 0.1 mM NADPH
0.0047
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in the presence of 0.04 mM NADPH and 5 mM L-glutamine
0.007
alpha-ketoglutarate
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in the presence of a fixed concentration of NADPH, and varied concentrations of L-glutamine
0.01
alpha-ketoglutarate
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in the presence of a fixed concentration of NADH, and varied concentrations of L-glutamine
0.012
alpha-ketoglutarate
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in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADH
0.013
alpha-ketoglutarate
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in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADPH
0.102
L-glutamine
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in the presence of a fixed concentration of NADPH, and varied concentrations of alpha-ketoglutarate
0.108
L-glutamine
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in the presence of a fixed concentration of NADH, and varied concentrations of alpha-ketoglutarate
0.115
L-glutamine
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in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADPH
0.12
L-glutamine
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in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADH
0.69
L-glutamine
dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 2.5 mM 2-oxoglutarate, and 0.1 mM NADPH
2.1
L-glutamine
hexameric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 2.5 mM 2-oxoglutarate, and 0.1 mM NADPH
0.091
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in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate
0.113
NADH
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in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine
0.0022
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in the presence of 1 mM alpha-ketoglutarate and 5 mM L-glutamine
0.0035
NADPH
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of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: iodonitrotetrazolium
0.006
NADPH
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in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate
0.007
NADPH
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in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine
0.0098
NADPH
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of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: menadione
0.0118
NADPH
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of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: ferricyanide
0.084
NADPH
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of NADPH: iodonitrotetrazolium oxidoreductase activity of the G298A-beta subunit
0.175
NADPH
dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 5 mM 2-oxoglutarate
0.245
NADPH
hexameric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 5 mM 2-oxoglutarate
additional information
steady-state kinetic analysis, overview
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additional information
additional information
steady-state kinetic analysis, overview
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additional information
additional information
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steady-state kinetic analysis, overview
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