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
-
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)
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Substrates Products
Substrates Products on EC 1.4.1.13 - glutamate synthase (NADPH)
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REACTION DIAGRAM
iodonitrotetrazolium + NADPH + H+
reduced iodonitrotetrazolium + NADP+
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-
-
-
r
L-glutamate + NADP+ + H2O
NH3 + 2-oxoglutarate + NADPH + H+
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-
-
?
L-glutamine + 2-oxoglutarate + acetylpyridine-NADPH + H+
L-glutamate + acetylpyridine-NADP+
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-
-
-
r
L-glutamine + 2-oxoglutarate + thio-NADPH + H+
L-glutamate + thio-NADP+
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-
-
-
r
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+ + H2O
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
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main route for assimilation of ammonium compounds
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?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
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glutamate biosynthesis
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?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
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main route for assimilation of ammonium compounds
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?
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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when L-glutamine is replaced by ammonia as the amino-group donor, the catalytic activity is less than 1%
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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2-oxoglutarate promotes electron transfer from FAD to 3Fe-4S cluster of the holoenzyme
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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highly specific
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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ammonia does not replace L-glutamine as amino donor
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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highly specific
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ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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L-glutamine, 2-oxoglutarate and NADPH are all required for catalytic activity
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ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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both native and apoglutamate synthase catalyze NADP+ reduction at approximately 12% the rate of NADPH oxidation
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r
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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highly specific
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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ammonia does not replace L-glutamine as amino donor
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions
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-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions
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-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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no activity with NH4+
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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-
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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NH3-dependent activity is increased approximately 5-fold in apoglutamate synthase lacking flavin and non-heme iron
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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highly specific
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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glyoxylate shows 3% reactivity compared with alpha-ketoglutarate
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?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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ammonia does not replace L-glutamine as amino donor
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?
L-glutamate + NADP+
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14% relative activity to L-glutamine
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?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
24% relative activity to L-glutamine with NADPH as electron donor and 6.3% relative activity to L-glutamine with NADH as electron donor
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?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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the specific activity of native enzyme using NH3 varies between 5% and 7% of the glutamine-dependent activity
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?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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the rate is only 10% to 15% that of the L-glutamine-dependent reaction
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?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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2% to 4% relative activity to L-glutamine
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?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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the activity with 10 mM NH4+ ions is less than 2% that with L-glutamine
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?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
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ammonia activity with 100 mM NH4Cl is about 6% of the glutamine activity with 5 mM L-glutamine
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?
?
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the enzyme beta subunit is devoid of glutamate synthase activity in either direction at both pH 7.5 and 9.5, but it can oxidize NADPH and transfer electrons to synthetic electron acceptors like iodonitrotetrazolium, ferricyanide, menadione, dichloroindophenol, the beta subunit is highly specific toward NADPH, the rate of oxidation of NADH in the presence of electron acceptors is less than 5% of that measured with NADPH
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?
additional information
?
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the recombinant enzyme has diaphorase activity, it can oxidize NADPH and transfer electrons to synthetic electron acceptors like iodonitrotetrazolium and ferricyanide
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?
additional information
?
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under conditions of physiological pH the enzyme exhibits a reversible half-reaction, but overall catalysis is essentially irreversible
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?
additional information
?
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the alpha subunit catalyzes the synthesis of glutamate from L-glutamine and 2-oxoglutarate, provided that a reducing system is present, reducing system: dithionite and methyl viologen
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-
?
additional information
?
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the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole
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-
?
additional information
?
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the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole
-
-
?
additional information
?
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-
the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole
-
-
?
additional information
?
-
the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole
-
-
?
additional information
?
-
the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole
-
-
?
additional information
?
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-
NH4Cl, L-asparagine, D-glutamine, or alkylated glutamine analogues do not substitute for L-glutamine, pyruvate or oxalacetate do not substitute for alpha-ketoglutarate
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-
?
additional information
?
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-
NH3-dependent activity is increased approximately 5fold in apoglutamate synthase lacking flavin and non-heme iron
-
-
?
additional information
?
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-
amino acids, amines and ammonium chloride do not substitute for L-glutamine, other alpha-keto acids including oxalacetate, pyruvate, glyoxylate and alpha-ketobutyrate do not support the activity
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-
?
additional information
?
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glutamine binding site of the enzyme is located on the heavy subunit of the enzyme, preparations of the enzyme that lack flavins or the flavins and iron sulfide catalyze NH3-dependent reaction but not glutamine-dependent reaction
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?
additional information
?
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assay with artificial eelectron acceptor iodonitrotetrazolium chloride
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?
additional information
?
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assay with artificial eelectron acceptor iodonitrotetrazolium chloride
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?
additional information
?
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assay with artificial eelectron acceptor iodonitrotetrazolium chloride
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?
additional information
?
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-
alpha-ketoglutarate can not be replaced with pyruvate or oxalacetate
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?