1.4.1.13 ferricyanide + NADPH + H+ - Azospirillum brasilense ferrocyanide + NADP+ - r 451560 1.4.1.13 iodonitrotetrazolium + NADPH + H+ - Azospirillum brasilense reduced iodonitrotetrazolium + NADP+ - r 451561 1.4.1.13 L-glutamate + NADP+ + H2O - Pyrococcus horikoshii NH3 + 2-oxoglutarate + NADPH + H+ - ? 424855 1.4.1.13 L-glutamine + 2-oxoglutarate + acetylpyridine-NADPH + H+ - Azospirillum brasilense L-glutamate + acetylpyridine-NADP+ - r 451558 1.4.1.13 L-glutamine + 2-oxoglutarate + NADH + H+ - Bacillus subtilis L-glutamate + NAD+ - r 440291 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH - Priestia megaterium L-glutamate + NADP+ - ? 370167 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH - Azospirillum brasilense L-glutamate + NADP+ - ? 370167 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH - Halobacillus halophilus L-glutamate + NADP+ - ? 370167 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH main route for assimilation of ammonium compounds Rhodospirillum rubrum L-glutamate + NADP+ - ? 370167 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH main route for assimilation of ammonium compounds Sclerotinia sclerotiorum L-glutamate + NADP+ - ? 370167 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH glutamate biosynthesis Rhodospirillum rubrum L-glutamate + NADP+ - ? 370167 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Pyrococcus sp. L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Bacillus subtilis L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Escherichia coli L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Klebsiella aerogenes L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Kluyveromyces marxianus L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Azospirillum brasilense L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Azospirillum brasilense L-glutamate + NADP+ - ir 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Rhodospirillum rubrum L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Oryza sativa L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ - Sclerotinia sclerotiorum L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ highly specific Escherichia coli L-glutamate + NADP+ - ir 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ highly specific [Brevibacterium] flavum L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ highly specific Bacillus licheniformis L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ highly specific Gluconobacter oxydans L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ glyoxylate shows 3% reactivity compared with alpha-ketoglutarate [Brevibacterium] flavum L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Escherichia coli L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Geobacillus stearothermophilus L-glutamate + NADP+ - ir 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Priestia megaterium L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Klebsiella aerogenes L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Bacillus licheniformis L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Amycolatopsis mediterranei L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Thiobacillus thioparus L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ when L-glutamine is replaced by ammonia as the amino-group donor, the catalytic activity is less than 1% Azospirillum brasilense L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ 2-oxoglutarate promotes electron transfer from FAD to 3Fe-4S cluster of the holoenzyme Azospirillum brasilense L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ NH3-dependent activity is increased approximately 5-fold in apoglutamate synthase lacking flavin and non-heme iron Thiobacillus thioparus L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ L-glutamine, 2-oxoglutarate and NADPH are all required for catalytic activity Escherichia coli L-glutamate + NADP+ - ir 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ both native and apoglutamate synthase catalyze NADP+ reduction at approximately 12% the rate of NADPH oxidation Escherichia coli L-glutamate + NADP+ - r 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ ammonia does not replace L-glutamine as amino donor Pseudomonas aeruginosa L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ ammonia does not replace L-glutamine as amino donor [Brevibacterium] flavum L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ ammonia does not replace L-glutamine as amino donor Bradyrhizobium sp. L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ no activity with NH4+ Rhodospirillum rubrum L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions Pyrococcus horikoshii L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions Pyrococcus horikoshii OT3 L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions Pyrococcus horikoshii OT-3 L-glutamate + NADP+ - ? 258908 1.4.1.13 L-glutamine + 2-oxoglutarate + thio-NADPH + H+ - Azospirillum brasilense L-glutamate + thio-NADP+ - r 451559 1.4.1.13 menadione + NADPH + H+ - Azospirillum brasilense menadiol + NADP+ - r 405813 1.4.1.13 metronidazole + NADP+ - Clostridium saccharobutylicum ? + NADPH - ? 373847 1.4.1.13 metronidazole + NADP+ - Clostridium saccharobutylicum NCP262 ? + NADPH - ? 373847 1.4.1.13 additional information - Escherichia coli ? - ? 89 1.4.1.13 additional information 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 Azospirillum brasilense ? - ? 89 1.4.1.13 additional information NH4Cl, L-asparagine, D-glutamine, or alkylated glutamine analogues do not substitute for L-glutamine, pyruvate or oxalacetate do not substitute for alpha-ketoglutarate Escherichia coli ? - ? 89 1.4.1.13 additional information the recombinant enzyme has diaphorase activity, it can oxidize NADPH and transfer electrons to synthetic electron acceptors like iodonitrotetrazolium and ferricyanide Azospirillum brasilense ? - ? 89 1.4.1.13 additional information NH3-dependent activity is increased approximately 5fold in apoglutamate synthase lacking flavin and non-heme iron Escherichia coli ? - ? 89 1.4.1.13 additional information 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 Klebsiella aerogenes ? - ? 89 1.4.1.13 additional information 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 Gluconobacter oxydans ? - ? 89 1.4.1.13 additional information alpha-ketoglutarate can not be replaced with pyruvate or oxalacetate Thiobacillus thioparus ? - ? 89 1.4.1.13 additional information under conditions of physiological pH the enzyme exhibits a reversible half-reaction, but overall catalysis is essentially irreversible Azospirillum brasilense ? - ? 89 1.4.1.13 additional information 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 Azospirillum brasilense ? - ? 89 1.4.1.13 additional information assay with artificial eelectron acceptor iodonitrotetrazolium chloride Pyrococcus horikoshii ? - ? 89 1.4.1.13 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 Entamoeba histolytica ? - ? 89 1.4.1.13 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 Entamoeba histolytica HM1:IMSS cl 6 ? - ? 89 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ - Pyrococcus sp. L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ - Escherichia coli L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ - Klebsiella aerogenes L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ the specific activity of native enzyme using NH3 varies between 5% and 7% of the glutamine-dependent activity Escherichia coli L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ 24% relative activity to L-glutamine with NADPH as electron donor and 6.3% relative activity to L-glutamine with NADH as electron donor Bacillus subtilis L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ the activity with 10 mM NH4+ ions is less than 2% that with L-glutamine Rhodospirillum rubrum L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ 2% to 4% relative activity to L-glutamine Priestia megaterium L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ ammonia activity with 100 mM NH4Cl is about 6% of the glutamine activity with 5 mM L-glutamine Thiobacillus thioparus L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ the rate is only 10% to 15% that of the L-glutamine-dependent reaction Geobacillus stearothermophilus L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ 14% relative activity to L-glutamine Amycolatopsis mediterranei L-glutamate + NADP+ - ? 258909 1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ - Pyrococcus horikoshii L-glutamate + NADP+ + H2O - ? 424945