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Information on EC 1.4.1.13 - glutamate synthase (NADPH)
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1.4.1.13 glutamate synthase (NADPH)IUBMB Comments
Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, alpha and beta. The alpha subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The beta subunit transfers electrons from the cosubstrate. The NH3 is channeled within the alpha subunit through a 31 A channel. The chanelling is very efficient and in the intact alpha-beta complex ammonia is produced only within the complex. In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can leak.
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Word Map
- 1.4.1.13
- nitrate
- ammonia
- seedling
- no3
-
ferredoxin-dependent
- chlorophyll
- shoot
- ferredoxin
-
6.3.1.2
-
iron-sulfur
-
nadh-dependent
- azaserine
- nitrogenase
-
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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
+
=
+
+
+
Synonyms
glutamate synthase, gogat, nadph-dependent glutamate synthase, nadph-gogat, l-glutamate synthase, ehno1, ehno2, glutamate synthase (nadph), gltb1, gltb2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.6.1.53
-
-
formerly
-
EhNO1
EhNO2
gltA
gltB
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-glutamate synthase
-
-
-
-
NADPH-GOGAT
NADPH-linked glutamate synthase
-
-
-
-
PH0876
synthase, glutamate (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
NADPH-dependent glutamate synthase
-
-
-
-
NADPH-GOGAT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate + NADP+ + H2O = NH3 + 2-oxoglutarate + NADPH + H+
1b
-
-
-
L-glutamate + NH3 = L-glutamine + H2O
1a
-
-
-
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
mechanism
-
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
mechanism
-
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
kinetic mechanism
-
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
hexa-uni ping pong mechanism
-
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (transaminating)
Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, alpha and beta. The alpha subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The beta subunit transfers electrons from the cosubstrate. The NH3 is channeled within the alpha subunit through a 31 A channel. The chanelling is very efficient and in the intact alpha-beta complex ammonia is produced only within the complex. In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can leak.
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CAS REGISTRY NUMBER
COMMENTARY
37213-53-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
iodonitrotetrazolium + NADPH + H+
reduced iodonitrotetrazolium + NADP+
-
-
-
-
r
L-glutamate + NADP+ + H2O
NH3 + 2-oxoglutarate + NADPH + H+
-
-
-
?
L-glutamine + 2-oxoglutarate + acetylpyridine-NADPH + H+
L-glutamate + acetylpyridine-NADP+
-
-
-
-
r
L-glutamine + 2-oxoglutarate + thio-NADPH + H+
L-glutamate + thio-NADP+
-
-
-
-
r
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+ + H2O
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
main route for assimilation of ammonium compounds
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
glutamate biosynthesis
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
main route for assimilation of ammonium compounds
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
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+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
when L-glutamine is replaced by ammonia as the amino-group donor, the catalytic activity is less than 1%
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
2-oxoglutarate promotes electron transfer from FAD to 3Fe-4S cluster of the holoenzyme
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
highly specific
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
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+
-
ammonia does not replace L-glutamine as amino donor
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
highly specific
-
ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
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 and NADPH are all required for catalytic activity
-
ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
both native and apoglutamate synthase catalyze NADP+ reduction at approximately 12% the rate of NADPH oxidation
-
r
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
ir
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
highly specific
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
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+
-
in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
ammonia does not replace L-glutamine as amino donor
-
?
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
-
-
?
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+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
no activity with NH4+
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
in the reverse reaction ammonia can act instead of glutamine, but more slowly
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
NH3-dependent activity is increased approximately 5-fold in apoglutamate synthase lacking flavin and non-heme iron
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
highly specific
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
glyoxylate shows 3% reactivity compared with alpha-ketoglutarate
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
ammonia does not replace L-glutamine as amino donor
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
14% relative activity to L-glutamine
-
?
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
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
the specific activity of native enzyme using NH3 varies between 5% and 7% of the glutamine-dependent activity
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
the rate is only 10% to 15% that of the L-glutamine-dependent reaction
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
2% to 4% relative activity to L-glutamine
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
the activity with 10 mM NH4+ ions is less than 2% that with L-glutamine
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
ammonia activity with 100 mM NH4Cl is about 6% of the glutamine activity with 5 mM L-glutamine
-
?
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
-
-
?
additional information
?
-
-
the recombinant enzyme has diaphorase activity, it can oxidize NADPH and transfer electrons to synthetic electron acceptors like iodonitrotetrazolium and ferricyanide
-
-
?
additional information
?
-
-
under conditions of physiological pH the enzyme exhibits a reversible half-reaction, but overall catalysis is essentially irreversible
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
NH4Cl, L-asparagine, D-glutamine, or alkylated glutamine analogues do not substitute for L-glutamine, pyruvate or oxalacetate do not substitute for alpha-ketoglutarate
-
-
?
additional information
?
-
-
NH3-dependent activity is increased approximately 5fold in apoglutamate synthase lacking flavin and non-heme iron
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
assay with artificial eelectron acceptor iodonitrotetrazolium chloride
-
-
?
additional information
?
-
assay with artificial eelectron acceptor iodonitrotetrazolium chloride
-
-
?
additional information
?
-
-
assay with artificial eelectron acceptor iodonitrotetrazolium chloride
-
-
?
additional information
?
-
-
alpha-ketoglutarate can not be replaced with pyruvate or oxalacetate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate + NADP+ + H2O
NH3 + 2-oxoglutarate + NADPH + H+
-
-
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+ + H2O
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
main route for assimilation of ammonium compounds
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
glutamate biosynthesis
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
main route for assimilation of ammonium compounds
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
the [4Fe-4S]+1,+2 cluster A displays three Cys and one Glu ligands for the Fe atoms. Residues Cys105 and Cys60 are linked to Fe1 and Fe2, respectively and the Fe3 atom shows bidentate coordination to Glu125 carboxylate, Fe4 is coordinated to Cys99, whose Calpha atom falls 5 A from FAD dimethyl-benzene ring C8 methyl. All Cys ligands to the [4Fe-4S]+1,+2 cluster B (Cys48, Cys51, Cys56, Cys109) are comprised in small subunit GltD loops at the interface with GltB
FAD
the isoalloxazine ring is almost solvent inaccessible, neighboring residues are Ile98, Pro100, Leu186, Ile191, Lys195, Leu266, Asp300, Thr301, Asp304, Leu450 and Val451, together with backbone atoms of the surrounding regions
flavin
-
0.86 mol FAD per mol of mutant beta subunit, 0.83 mol FAD per mol of the wild type species
flavin
-
the alpha subunit contains FMN as flavin cofactor, 0.94 FMN bound per alpha subunit
flavin
-
the beta subunit contains the binding site for FAD, 0.83 mol FAD per mol beta subunit
NADPH
-
the C-terminal potential ADP-binding fold of the beta subunit is the NADPH-binding site of the enzyme
NADPH
-
the beta subunit contains the NADPH binding site of the enzyme
additional information
-
the enzyme contains three distinct ion-sulfur centers per alphabeta protomer
-
additional information
-
the enzyme contains 8.1 acid-labile sulfur atoms per 220000-dalton dimer
-
additional information
-
the enzyme contains three different iron-sulfur clusters, one 3Fe-4S center on the alpha subunit and two 4Fe-4S clusters of unknown location, 11.7 mol sulfur per mol alphabeta protomer
-
additional information
-
purified enzyme contains 30.4 mol of labile sulfide per 800,000 g of protein
-
additional information
-
the alpha subunit contains the [3Fe-4S] cluster of the enzyme
-
additional information
-
midpoint potential value of the FMN cofactor: approximately -240 mV, midpoint potential value of the 3Fe-4S cluster: approximately -270 mV, midpoint potential value of the FAD cofactor: approximately -340 mV for the beta subunit and -300 mV for the holoenzyme
-
additional information
-
the FMN and FAD prosthetic groups are demonstrated to be nonequivalent with respect to their reactivities with sulfite, sulfite reacts with only one of the two flavins forming an N(5)-sulfite adduct
-
additional information
-
thio-NADPH and acetylpyridine-NADPH can be used as electron donors but are less efficient than NADPH
-
additional information
-
the enzyme contains 7.9 sulfur atoms per protomer with a molecular weight of 185000
-
additional information
-
the enzyme contains 7.2 mol of acid-labile sulfur per 200,000 g of protein
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
additional information