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
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assimilatory
- alpha-ketoglutarate
- brasilense
-
amidotransferase
- glutaminase
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hydroponic
-
photorespiratory
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photorespiration
-
15n-labeled
-
n2-fixing
- molecular biology
-
nadp-glutamate
- heterocysts
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glutamine-dependent
-
ureides
Reaction
2 L-glutamate
+
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
1.4.1.13 glutamate synthase (NADPH)Advanced search results
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results (Inhibitors
Inhibitors on EC 1.4.1.13 - glutamate synthase (NADPH)
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2',5'-diphosphoadenylic acid
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competitive inhibitor with respect to NADPH
2'-phosphoadenylic acid
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competitive inhibitor with respect to NADPH
iodonitrotetrazolium
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inhibitor of the L-glutamate:iodonitrotetrazolim oxidoreductase activity of the alpha subunit at concentrations above 0.1 mM
NAD+
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competitive inhibition with NADH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine
oxalylglycine
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competitive inhibitor vs. alpha-ketoglutarate, noncompetitive inhibitor vs. L-glutamine and uncompetitive vs. NADPH
p-chloromercuriphenylsulfonate
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more than 50% loss in activity in 60 min at 0.05 mM
Phenylglyoxal
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at 3 mM pyridoxal 5'-phosphate glutamine-dependent glutamate synthase is inactivated by about 50% within 10 min. This inactivation is not prevented by 2-oxoglutarate
pyridoxal-5'-phosphate
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52% inhibition of the glutamine-dependent reaction at 5 mM
2'-adenylic acid
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competitive inhibitor of the forward reaction with NADPH as the varied substrate, uncompetitive inhibitor with alpha-ketoglutarate or L-glutamine
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
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for the NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, uncompetitive inhibition with ferricyanide or iodonitrotetrazolium as substrate, competitive inhibition with NADPH as substrate
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
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inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH
3-Aminopyridine adenine dinucleotide phosphate
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good inhibitor of the holoenzyme, competitive with respect to NADPH
3-Aminopyridine adenine dinucleotide phosphate
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inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH
4-Iodoacetamidosalicylate
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inactivation is faster at pH 4.6 to 5.5 compared to pH 6.5 to 7.2
6-diazo-5-oxo-L-norleucine
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potent inhibitor, complete loss of activity at 0.1 mM after 10 min of preincubation
6-diazo-5-oxo-L-norleucine
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35% inhibition at 0.0025 mM, when reaction is initiated with 0.5 mM L-glutamine, 73% inhibition at 0.0025 mM, when reaction is initiated with 2.5 mM 2-oxoglutarate
azaserine
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in both the L-glutamine- and NH4Cl-dependent reactions
azaserine
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38% inhibition at 0.0125 mM when reaction is initiated with 0.5 mM L-glutamine and 69% inhibition at 0.0125 mM when reaction is initiated with 2.5 mM 2-oxoglutarate
D-glutamate
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competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with L-glutamine and uncompetitive with NADPH
iodoacetate
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completely inhibits at 1 mM, 2-mercaptoethanol protects against inhibition
L-2-Amino-4-oxo-5-chloropentanoic acid
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selective inhibitor of glutamine-dependent activity
L-2-Amino-4-oxo-5-chloropentanoic acid
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selective inhibitor of glutamine-dependent activity
L-asparagine
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activity decreases to about 0.5% of the original at 25 mM
L-glutamate
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noncompetitive inhibitor with respect to both 2-oxoglutarate and L-glutamine
L-glutamate
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competitive inhibitor of the forward reaction with L-glutamine as the varied substrate, noncompetitive inhibitor with alpha-ketoglutarate as the varied substrate
L-methionine sulfone
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competitive inhibitor vs. L-glutamine, noncompetitive inhibitor vs. alpha-ketoglutarate and uncompetitive vs. NADPH
NADP+
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inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH
NADP+
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competitive inhibition with respect to NADPH; potent inhibitor
NADP+
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competitive inhibition with NADPH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine
NADPH
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inactivation of glutamine-dependent activity, 50% inactivation at 0.36 mM in 10 min
NADPH
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rapid inactivation in absence of L-glutamine and 2-oxoglutarate, capable of causing 50% inactivation in 5 min at a concentration of 1 mM
p-chloromercuribenzoate
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completely inhibits at 1 mM, 2-mercaptoethanol protects against inhibition
additional information
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relatively insensitive to inhibition by amino acids, keto acids or various nucleotides, 38% inhibition with a combination of each 5 mM L-methionine, L-leucine, L-serine, L-histidine, L-glycine and L-alanine
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additional information
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a combination of L-serine, L-methionine, L-alanine, L-glycine, L-histidine and L-asparagine inhibits 73% of the acitivity at 7.5 mM each
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