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ferricyanide + NADPH + H+
ferrocyanide + NADP+
-
-
-
-
r
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 + NADH + H+
L-glutamate + NAD+
-
-
-
-
r
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
L-glutamine + 2-oxoglutarate + thio-NADPH + H+
L-glutamate + thio-NADP+
-
-
-
-
r
menadione + NADPH + H+
menadiol + NADP+
-
-
-
-
r
metronidazole + NADP+
? + NADPH
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+ + H2O
-
-
-
?
additional information
?
-
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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
-
?
metronidazole + NADP+
? + NADPH
-
-
-
?
metronidazole + NADP+
? + NADPH
-
-
-
?
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+
-
-
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
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+
-
-
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
2% to 4% relative activity to L-glutamine
-
?
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
-
-
-
?
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
?
-
-
-
-
-
?
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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2',5'-ADP
-
act as a competitive ihibitor
2',5'-diphosphoadenylic acid
-
competitive inhibitor with respect to NADPH
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
2'-phosphoadenylic acid
-
competitive inhibitor with respect to NADPH
3-Aminopyridine adenine dinucleotide phosphate
3-Bromo-2-oxoglutarate
-
-
4-Iodoacetamidosalicylate
6-diazo-5-oxo-L-norleucine
AgNO3
-
at 0.001 mM completely inhibits
arginine
-
less than 45% inhibition
Atebrin
-
100% inhibition at 1 mM
BaCl2
-
61% inhibition at 50 mM
Butane-2,3-dione
-
slight inactivation
CdCl2
-
produces more than 60% inhibition at 5 mM
cis-aconitate
-
22% inhibition at 50 mM
CoCl2
-
produces more than 60% inhibition at 5 mM
CTP
-
9% inhibition at 25 mM and 21% inhibition at 50 mM
D-Lysine
-
significantly inhibits
D-methionine
-
19% inhibition at 50 mM
dimethyl suberimidate
-
inactivates glutamine-dependent activity
DL-methionine DL-sulfoximine
DL-methionine sulfoxide
-
potent inhibitor
GTP
-
16% inhibition at 25 mM and 43% inhibition at 50 mM
HgCl2
-
at 0.001 mM remains 8% of activity
iodonitrotetrazolium
-
inhibitor of the L-glutamate:iodonitrotetrazolim oxidoreductase activity of the alpha subunit at concentrations above 0.1 mM
ITP
-
17% inhibition at 25 mM and 29% inhibition at 50 mM
KCl
-
32% inhibition at 100 mM
KCN
-
89% inhibition at 20 mM
KNO3
-
47% inhibition at 100 mM
L-2-Amino-4-oxo-5-chloropentanoic acid
L-cysteine
-
significant inhibitor
L-methionine DL-sulfoximine
L-tryptophan
-
strong inhibitor
NAD+
-
competitive inhibition with NADH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine
NaN3
-
100% inhibition at 50 mM, 11% inhibition at 20 mM
NiCl2
-
produces more than 60% inhibition at 5 mM
O-carbamoylserine
-
competitive inhibitor vs. L-glutamine
oxalate
-
48% inhibition at 5 mM
oxalylglycine
-
competitive inhibitor vs. alpha-ketoglutarate, noncompetitive inhibitor vs. L-glutamine and uncompetitive vs. NADPH
p-chloromercuriphenylsulfonate
-
more than 50% loss in activity in 60 min at 0.05 mM
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM, 5 min
Phenylglyoxal
-
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
-
52% inhibition of the glutamine-dependent reaction at 5 mM
UTP
-
17% inhibition at 25 mM and 33% inhibition at 50 mM
2'-adenylic acid
-
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
-
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
-
inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
-
-
2,2'-bipyridyl
-
88% inhibition at 10 mM
2,2'-bipyridyl
-
100% inhibition at 3 mM
3-Aminopyridine adenine dinucleotide phosphate
-
good inhibitor of the holoenzyme, competitive with respect to NADPH
3-Aminopyridine adenine dinucleotide phosphate
-
inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH
3-Aminopyridine adenine dinucleotide phosphate
-
-
4-Iodoacetamidosalicylate
-
inactivation is faster at pH 4.6 to 5.5 compared to pH 6.5 to 7.2
4-Iodoacetamidosalicylate
-
-
6-diazo-5-oxo-L-norleucine
-
potent inhibitor, complete loss of activity at 0.1 mM after 10 min of preincubation
6-diazo-5-oxo-L-norleucine
-
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
ADP
-
15% inhibition at 50 mM
ATP
-
19% inhibition at 25 mM and 43% inhibition at 50 mM
ATP
-
restricts activity by 47% at 5 mM
ATP
-
33% inhibition at 20 mM
ATP
-
at 3.5 mM 12% inhibition
azaserine
-
in both the L-glutamine- and NH4Cl-dependent reactions
azaserine
-
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
azaserine
-
68% inhibition at 1 mM
CaCl2
-
-
CaCl2
-
27% inhibition at 50 mM
CaCl2
-
74% inhibition at 50 mM
D-glutamate
-
-
D-glutamate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with L-glutamine and uncompetitive with NADPH
D-glutamate
-
no inhibition: 50-200 mM
D-glutamate
-
50% inhibition at concentrations below 7 mM
D-glutamate
-
at 3.5 mM 10% inhibition
DL-methionine DL-sulfoximine
-
-
DL-methionine DL-sulfoximine
-
potent inhibitor
DL-methionine DL-sulfoximine
-
-
fumarate
-
potent inhibitor of the glutamine-dependent activity
fumarate
-
21% inhibition at 50 mM
glycine
-
less than 50% inhibition at 5 mM
glycine
-
5% inhibition at 5 mM
glycine
-
significant inhibitor
iodoacetamide
-
more than 50% loss in activity in 60 min at 0.5 mM
iodoacetamide
-
selective inactivation of glutamine-dependent activity
iodoacetate
-
27% inhibition at 25 mM
iodoacetate
-
completely inhibits at 1 mM, 2-mercaptoethanol protects against inhibition
isocitrate
-
35% inhibition at 5 mM
isocitrate
-
35% inhibition at 50 mM
isocitrate
-
32% inhibition at 20 mM
KBr
-
-
KBr
-
43% inhibition at 100 mM
L-2-Amino-4-oxo-5-chloropentanoic acid
-
selective inhibitor of glutamine-dependent activity
L-2-Amino-4-oxo-5-chloropentanoic acid
-
selective inhibitor of glutamine-dependent activity
L-alanine
-
less than 50% inhibition at 5 mM
L-alanine
-
5% inhibition at 5 mM
L-alanine
-
significant inhibitor
L-asparagine
-
less than 50% inhibition at 5 mM
L-asparagine
-
activity decreases to about 0.5% of the original at 25 mM
L-asparagine
-
significant inhibitor
L-aspartate
-
50% inhibition at concentrations below 7 mM
L-glutamate
-
potent inhibitor
L-glutamate
-
noncompetitive inhibitor with respect to both 2-oxoglutarate and L-glutamine
L-glutamate
-
30% inhibition at 500 mM
L-glutamate
-
50% inhibition at concentrations between 17 and 35 mM
L-glutamate
-
competitive inhibitor of the forward reaction with L-glutamine as the varied substrate, noncompetitive inhibitor with alpha-ketoglutarate as the varied substrate
L-glutamate
-
more than 40% inhibition at 50 mM
L-glutamate
-
at 3.5 mM 13% inhibition
L-histidine
-
less than 50% inhibition at 5 mM
L-histidine
-
5% inhibition at 5 mM
L-histidine
-
significant inhibitor
L-histidine
-
more than 40% inhibition at 50 mM
L-histidine
-
significant inhibitor
L-homoserine
-
significant inhibitor
L-homoserine
-
significant inhibitor
L-leucine
-
less than 50% inhibition at 5 mM
L-leucine
-
16% inhibition at 5 mM
L-leucine
-
less than 45% inhibition
L-malate
-
more than 50% inhibition at 5 mM
L-malate
-
potent inhibitor of the glutamine-dependent activity
L-malate
-
19% inhibition at 50 mM
L-malate
-
40% inhibition at 5 mM
L-malate
-
at 3.5 mM 67% inhibition
L-methionine
-
shows no effect
L-methionine
-
competitive inhibitor with respect to L-glutamine
L-methionine
-
16% inhibition at 5 mM
L-methionine
-
50% inhibition at concentrations below 7 mM
L-methionine
-
more than 40% inhibition at 50 mM
L-methionine DL-sulfoximine
-
potent inhibitor
L-methionine DL-sulfoximine
-
inhibits the glutamine-dependent reaction
L-methionine sulfone
-
reversible inhibitor
L-methionine sulfone
-
potent inhibitor
L-methionine sulfone
-
competitive inhibitor vs. L-glutamine, noncompetitive inhibitor vs. alpha-ketoglutarate and uncompetitive vs. NADPH
L-serine
-
less than 50% inhibition at 5 mM
L-serine
-
10% inhibition at 5 mM
L-serine
-
significant inhibitor
L-serine
-
more than 40% inhibition at 10 mM and 50 mM
lysine
-
-
lysine
-
significantly inhibits
MgCl2
-
31% inhibition at 50 mM
MgCl2
-
70% inhibition at 50 mM
MnCl2
-
64% inhibition at 50 mM
MnCl2
-
82% inhibition at 50 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
83% inhibition at 10 mM
NADH
-
partially inhibits
NADH
-
at 3.5 mM 31% inhibition
NADP+
-
potent inhibitor
NADP+
-
inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH
NADP+
-
competitive inhibition with respect to NADPH; potent inhibitor
NADP+
-
competitive inhibition with NADPH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine
NADP+
-
50% inhibition at concentrations below 7 mM
NADP+
-
competitive vs. NADPH and noncompetitive vs. L-glutamine
NADP+
-
competitive inhibitor with NADPH, 54% inhibition at 1 mM
NADP+
-
59% inhibition at 1 mM
NADPH
-
-
NADPH
-
inactivation of glutamine-dependent activity, 50% inactivation at 0.36 mM in 10 min
NADPH
-
rapid inactivation in absence of L-glutamine and 2-oxoglutarate, capable of causing 50% inactivation in 5 min at a concentration of 1 mM
o-phenanthroline
-
complete inhibition at 10 mM
o-phenanthroline
-
37% inhibition at 10 mM
oxaloacetate
-
-
oxaloacetate
-
more than 50% inhibition at 20 mM
p-chloromercuribenzoate
-
inhibits the glutamine-dependent reaction
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
complete inhibition at 0.1 mM
p-chloromercuribenzoate
-
completely inhibits at 1 mM, 2-mercaptoethanol protects against inhibition
phenylalanine
-
78% inhibition at 10 mM
phenylalanine
-
significantly inhibits
pyruvate
-
20% inhibition at 50 mM
sodium arsenite
-
57% inhibition at 10 mM
sodium arsenite
-
100% inhibition at 50 mM , 10% inhibition at 20 mM
succinate
-
25% inhibition at 5 mM
succinate
-
16% inhibition at 50 mM
valine
-
-
valine
-
less than 45% inhibition
additional information
-
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
-
additional information
-
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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0.017
acetylpyridine-NADPH
-
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
0.0047 - 0.35
alpha-ketoglutarate
0.14
ferricyanide
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.05
iodonitrotetrazolium
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.035
menadione
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.01
thio-NADPH
-
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
additional information
additional information
-
0.009
2-oxoglutarate
-
-
0.23
2-oxoglutarate
dimeric enzyme, at 25Ā°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
-
NH3-dependent glutamate synthase and apoglutamate synthase
0.75
2-oxoglutarate
hexameric enzyme, at 25Ā°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
alpha-ketoglutarate
-
in the presence of 0.04 mM NADPH and 5 mM L-glutamine
0.007
alpha-ketoglutarate
-
in the presence of a fixed concentration of NADPH, and varied concentrations of L-glutamine
0.0073
alpha-ketoglutarate
-
-
0.0086
alpha-ketoglutarate
-
-
0.01
alpha-ketoglutarate
-
in the presence of a fixed concentration of NADH, and varied concentrations of L-glutamine
0.012
alpha-ketoglutarate
-
in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADH
0.013
alpha-ketoglutarate
-
in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADPH
0.05
alpha-ketoglutarate
-
-
0.053
alpha-ketoglutarate
-
-
0.06
alpha-ketoglutarate
-
-
0.3
alpha-ketoglutarate
-
-
0.35
alpha-ketoglutarate
-
-
0.029
L-glutamine
-
-
0.102
L-glutamine
-
in the presence of a fixed concentration of NADPH, and varied concentrations of alpha-ketoglutarate
0.108
L-glutamine
-
in the presence of a fixed concentration of NADH, and varied concentrations of alpha-ketoglutarate
0.115
L-glutamine
-
in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADPH
0.12
L-glutamine
-
in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADH
0.23
L-glutamine
-
holoenzyme, buffer: Hepes, pH 8.5 or 7.5
0.63
L-glutamine
-
alpha subunit, buffer: Hepes, pH 7.5
0.69
L-glutamine
dimeric enzyme, at 25Ā°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
0.73
L-glutamine
-
holoenzyme, buffer: CAPS, pH 9.5
0.92
L-glutamine
-
alpha subunit, buffer: Hepes, pH 8.5
1.5
L-glutamine
-
alpha subunit, buffer: CAPS, pH 9.5
2.1
L-glutamine
hexameric enzyme, at 25Ā°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
NADH
-
in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate
0.113
NADH
-
in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine
0.0022
NADPH
-
in the presence of 1 mM alpha-ketoglutarate and 5 mM L-glutamine
0.0035
NADPH
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: iodonitrotetrazolium
0.006
NADPH
-
in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate
0.007
NADPH
-
in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine
0.0098
NADPH
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: menadione
0.0118
NADPH
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: ferricyanide
0.014
NADPH
-
NH3-dependent glutamate synthase and apoglutamate synthase
0.042
NADPH
pH 7.5, 37Ā°C, pGLTY2
0.084
NADPH
-
of NADPH: iodonitrotetrazolium oxidoreductase activity of the G298A-beta subunit
0.11
NADPH
pH 7.5, 70Ā°C, pGLTY2
0.175
NADPH
dimeric enzyme, at 25Ā°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 25Ā°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
6.42
NADPH
pH 7.5, 37Ā°C, pGLTZ
16.3
NADPH
pH 7.5, 70Ā°C, pGLTZ
0.5 - 2
NH4Cl
-
-
additional information
additional information
steady-state kinetic analysis, overview
-
additional information
additional information
steady-state kinetic analysis, overview
-
additional information
additional information
-
steady-state kinetic analysis, overview
-
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0.048
2',5'-diphosphoadenylic acid
-
-
2.1 - 17.2
2'-adenylic acid
0.0028
2'-phosphoadenosine 5'-diphospho-5-beta-D-ribose
-
-
0.021 - 0.495
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
0.0227 - 0.233
2'-phosphoadenosine-5'-diphosphoribose
0.186
2'-phosphoadenylic acid
-
-
0.0024 - 0.128
3-Aminopyridine adenine dinucleotide phosphate
0.012
Cibacron blue 3GA
-
-
0.011 - 0.056
D-glutamate
0.02 - 0.76
DL-methionine DL-sulfoximine
0.025
L-2-Amino-4-oxo-5-chloropentanoic acid
-
-
1.05
L-methionine
-
competitive inhibitor with respect to L-glutamine
0.022
L-methionine sulfone
-
-
0.01 - 0.045
methionine sulfone
0.86
p-chloromercuribenzoate
-
-
additional information
additional information
-
2.1
2'-adenylic acid
-
competitive inhibitor with respect to NADPH
17.1
2'-adenylic acid
-
uncompetitive inhibitor with respect to glutamine
17.2
2'-adenylic acid
-
uncompetitive inhibitor with respect to alpha-keto-glutarate
0.021
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
-
for the NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, substrate: NADPH, cosubstrate: ferricyanide
0.08
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
-
for the NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, substrate: NADPH, cosubstrate: iodonitrotetrazolium
0.18
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
-
for the NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, substrate: ferricyanide, cosubstrate: NADPH
0.495
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
-
for the NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, substrate: iodonitrotetrazolium, cosubstrate: NADPH
0.0227
2'-phosphoadenosine-5'-diphosphoribose
-
inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of wild type-beta subunit
0.233
2'-phosphoadenosine-5'-diphosphoribose
-
inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit
0.0024
3-Aminopyridine adenine dinucleotide phosphate
-
-
0.0024
3-Aminopyridine adenine dinucleotide phosphate
-
inhibitor of the holoenzyme, competitive with NADPH
0.0112
3-Aminopyridine adenine dinucleotide phosphate
-
inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of wild type-beta subunit
0.128
3-Aminopyridine adenine dinucleotide phosphate
-
inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit
0.011
D-glutamate
-
good competitive inhibitor with respect to 2-oxoglutarate
0.044
D-glutamate
-
uncompetitive inhibitor with NADPH
0.056
D-glutamate
-
noncompetitive inhibitor with L-glutamine
0.02
DL-methionine DL-sulfoximine
-
competitive inhibitor with respect to alpha-keto-glutarate
0.14
DL-methionine DL-sulfoximine
-
competitive inhibitor with respect to glutamine
0.76
DL-methionine DL-sulfoximine
-
noncompetitive inhibitor with respect to NADPH
25
glutamate
-
competitive inhibitor with respect to glutamine
45
glutamate
-
competitive inhibitor with respect to alpha-ketoglutarate
0.48
methionine
-
competitive inhibitor with respect to alpha-keto-glutarate
3
methionine
-
competitive inhibitor with respect to glutamine
5.5
methionine
-
noncompetitive inhibitor with respect to NADPH
0.01
methionine sulfone
-
competitive inhibitor with respect to glutamine
0.041
methionine sulfone
-
uncompetitive inhibitor with respect to alpha-ketoglutarate
0.045
methionine sulfone
-
uncompetitive inhibitor with respect to NADPH
0.02
NADP
-
competitive inhibition with NADPH
0.07
NADP
-
competitive inhibition with NADPH
0.12
NADP
-
mixed-type inhibition with alpha-ketoglutarate
0.25
NADP
-
competitive inhibitor vs. NADPH
0.3
NADP
-
uncompetitive inhibition with respect to glutamine
0.69
NADP
-
uncompetitive inhibitor vs. alpha-ketoglutarate
1.13
NADP
-
uncompetitive inhibitor vs. glutamine
0.0059
NADP+
-
-
0.037
NADP+
-
inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit
0.8
oxalylglycine
-
competitive inhibitor with respect to alpha-ketoglutarate
19.3
oxalylglycine
-
uncompetitive inhibitor with respect to glutamine
20.6
oxalylglycine
-
uncompetitive inhibitor with respect to NADP
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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of the alpha subunit, using column chromatography on Q-Sepharose and Ultrogel AcA34
-
of the G298A-beta subunit, using column chromatography on Reactive Red or Amicon Red resins and gel filtration on Ultrogel AcA 34
-
of the recombinant enzyme beta subunit, using ammonium sulfate fractionation, affinity chromatography on Reactive Red, ultrafiltration and column chromatography on Ultrogel AcA 54
-
of the recombinant enzyme from overproducing Escherichia coli cells, using ion exchange chromatography on Q-Sepharose, gel filtration on Sephacryl S-300 and affinity chromatography on 2',5' ADP-Sepharose 4B colum
-
partial purification using column chromatography on DEAE-cellulose
-
partial, using ultrasonic oscillation, ammonium sulfate precipitation, column chromatography on Sephacryl S300 and DE-52 cellulose
-
recombuinant enzyme and isolated beta subunit
-
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose and Blue-Sepharose
-
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose and Sephadex G-200
-
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose, Sepharose 6B, hydroxyapatite, glutamate dehydrogenase antibody affinity chromatography and column chromatography on Sephacryl S-200
-
using ammonium sulfate fractionation, coulmn chromatography on DEAE-cellulose, hydroxyapatite, Sepharose 6B and Sephadex G-200
-
using ammonium sulfate fractionation, gel filtration on Sephacryl S-300 and affinity chromatography on NADPH-Sepharose
-
using ammonium sulfate precipitation and column chromatography on DEAE-Sepharose, 2',5'-ADP-Sepharose and Sephacryl S-300
-
using heat treatment, ammonium sulfate precipitation, column chromatography on DEAE-Trisacryl, gel filtration and affinity chromatogray
-
using heat treatment, anion-exchange column chromatography on HiTrap Q and cation exchange column chromatography on Resources S
-
using protamine sulfate precipitation, ammonium sulfate precipitation, column chromatography on DE52, DEAE-Sephadex, hydroxyapatite, phenyl-Sepharose CL-4B and Bio-Gel filtration
-
using sonication, heat treatment, protamine sulfate precipitation, ammonium sulfate precipitation, gel filtration on G-50, column chromatography on DEAE-Sephadex and gel filtration on Sephadex G-200 and Sepharose 6B
-
using streptomycin sulfate treatment, ammonium sulfate fractionation, heat treatment, agarose gel filtration and DEAE-cellulose column chromatography
-
using streptomycin sulfate treatment, ammonium sulfate precipitation, column chromatography on DEAE-Sephacel, Bio-Gel A 1.5 m, Red Sepharose CL6B and Sephadex G-25
-
using streptomycin sulfate treatment, ammonium sulfate precipitation, column chromatography on Ultrogel AcA 22 and DEAE-Sephadex A-50, ultrafiltration with an Amicon PM 30 membrane and chromatography on hydroxyapatite column
-
using sulfate precipitation, gel filtration and column chromatography on 2',5'-ADP-Sepharose
-
-
-
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Miller, R.E.; Stadtman, E.R.
Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein
J. Biol. Chem.
247
7407-7419
1972
Escherichia coli
brenda
Tempest, D.W.; Meers, J.L.
Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route
Biochem. J.
117
405-407
1970
Klebsiella aerogenes
brenda
Mei, B.; Jiao, R.
Purification and properties of glutamate synthase from Nocardia mediterranei
J. Bacteriol.
170
1940-1944
1988
Amycolatopsis mediterranei
brenda
Schmidt, C.N.G.; Jervis, L.
Affinity purification of glutamate synthase from Escherichia coli
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104
127-129
1980
Escherichia coli
brenda
Rendina, A.R.; Orme-Johnson, W.H.
Glutamate synthase: on the kinetic mechanism of the enzyme from Escherichia coli W
Biochemistry
17
5388-5393
1978
Escherichia coli
brenda
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The enzymes of the ammonia assimilation in Pseudomonas aeruginosa
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124
197-203
1980
Pseudomonas aeruginosa
brenda
Vanoni, M.A.; Edmondson, D.E.; Zanetti, G.; Curti, B.
Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism, and electron paramagnetic resonance spectroscopies
Biochemistry
31
4613-4623
1992
Azospirillum brasilense
brenda
Vanoni, M.A.; Edmondson, D.E.; Rescigno, M.; Zanetti, G.; Curti, B.
Mechanistic studies on Azospirillum brasilense glutamate synthase
Biochemistry
30
11478-11484
1991
Azospirillum brasilense
brenda
Ratti, S.; Curti, B.; Zanetti, G.; Galli, E.
Purification and characterization of glutamate synthase from Azospirillum brasilense
J. Bacteriol.
163
724-729
1985
Azospirillum brasilense
brenda
Sung, H.C.; Tachiki, T.; Kumagai, H.; Tochikura, T.
Properties of glutamate synthase from Brevibachterium flavum
J. Ferment. Technol.
62
569-575
1984
[Brevibacterium] flavum
-
brenda
Tachiki, T.; Sung, H.C.; Wakisaka, S.; Tochikura, T.
Purification and some properties of glutamate synthase from Gluconobacter subodydans on glutamate as a nitrogen source
J. Ferment. Technol.
61
179-184
1983
Gluconobacter oxydans
-
brenda
Schreier, H.J.; Bernlohr, R.W.
Purification and properties of glutamate synthase from Bacillus licheniformis
J. Bacteriol.
160
591-599
1984
Bacillus licheniformis
brenda
Suzuki, A.; Jacquot, J.P.; Gadal, P.
Glutamate synthase in rice roots. Studies on the electron donor specificity
Phytochemistry
22
1543-1546
1983
Oryza sativa
-
brenda
Schmidt, C.N.G.; Jervis, L.
Partial purification and characterization of glutamate synthase from a thermophilic bacillus
J. Gen. Microbiol.
128
1713-1718
1982
Geobacillus stearothermophilus
-
brenda
Yelton, M.M.; Yoch, D.C.
Nitrogen metabolism in Rhodospirillum rubrum: Characterization of glutamate synthase
J. Gen. Microbiol.
123
335-342
1981
Rhodospirillum rubrum
-
brenda
Nisbet, B.A.; Slaughter, J.C.
Glutamate dehydrogenase and glutamate synthase from the yeast Kluyveromyces fragilis: Variability in occurrence and properties
FEMS Microbiol. Lett.
7
319-321
1980
Kluyveromyces marxianus
-
brenda
Hemmilä, I.A.; Mäntsälä, P.I.
Purification and properties of glutamate synthase and glutamate dehydrogenase from Bacillus megaterium
Biochem. J.
173
45-52
1978
Priestia megaterium
brenda
Adachi, K.; Suzuki, I.
Purification and properties of glutamate synthase from Thiobacillus thioparus
J. Bacteriol.
129
1173-1182
1977
Thiobacillus thioparus
brenda
Mäntsälä, P.; Zalkin, H.
Properties of apoglutamate synthase and comparison with glutamate dehydrogenase
J. Biol. Chem.
251
3300-3305
1976
Escherichia coli
brenda
Mäntsälä, P.; Zalkin, H.
Glutamate synthase. Properties of the glutamine-dependent activity
J. Biol. Chem.
251
3294-3299
1976
Escherichia coli
brenda
Hua, S.S.T.; Lichens, G.M.; Guirao, A.; Tsai, V.Y.
Biochemical properties of glutamate synthase of salt-tolerant Bradyrhizobium sp. Strain WR1001
FEMS Microbiol. Lett.
37
209-213
1986
Bradyrhizobium sp.
-
brenda
Matsuoka, K.; Kimura, K.
Glutamate synthase from Bacillus subtilis PCI 219
J. Biochem.
99
1087-1100
1986
Bacillus subtilis
brenda
Meister, A.
Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae
Methods Enzymol.
113
327-337
1985
Escherichia coli, Klebsiella aerogenes
brenda
Rachim, M.A.; Nicholas, D.J.D.
Glutamine synthetase and glutamate synthase from Sclerotinia Schlerotiorum
Phytochemistry
24
2541-2548
1985
Sclerotinia sclerotiorum
-
brenda
Carlberg, I.; Norlund, S.
Purification and partial characterization of glutamate synthase from Rhodospirillum rubrum grown under nitrogen-fixing conditions
Biochem. J.
279
151-154
1991
Rhodospirillum rubrum
brenda
Vanoni, M.A.; Verzotti, E.; Zanetti, G.; Curti, B.
Properties of the recombinant beta subunit of glutamate synthase
Eur. J. Biochem.
236
937-946
1996
Azospirillum brasilense
brenda
Jongsareejit, B.; Rahman, R.N.Z.A.; Fujiwara, S.; Imanaka, T.
Gene cloning, sequencing and enzymic properties of glutamate synthase from the hyperthermophilic archaeon Pyrococcus sp. KOD1
Mol. Gen. Genet.
254
635-642
1997
Pyrococcus sp.
brenda
Vanoni, M.A.; Fischer, F.; Ravasio, S.; Verzotti, E.; Edmondson, D.E.; Hagen, W.R.; Zanetti, G.; Curti, B.
The recombinant alpha subunit of glutamate synthase: spectroscopic and catalytic properties
Biochemistry
37
1828-1838
1998
Azospirillum brasilense
brenda
Morandi, P.; Valzasina, B.; Colombo, C.; Curti, B.; Vanoni, M.A.
Glutamate Synthase: Identification of the NADPH-Binding Site by Site-Directed Mutagenesis
Biochemistry
39
727-735
2000
Azospirillum brasilense
brenda
Stabile, H.; Curti, B.; Vanoni, M.A.
Functional properties of recombinant Azospirillum brasilense glutamate synthase, a complex iron-sulfur flavoprotein
Eur. J. Biochem.
267
2720-2730
2000
Azospirillum brasilense
brenda
Ravasio, S.; Curti, B.; Vanoni, M.A.
Determination of the Midpoint Potential of the FAD and FMN Flavin Cofactors and of the 3Fe-4S Cluster of Glutamate Synthase
Biochemistry
40
5533-5541
2001
Azospirillum brasilense
brenda
Ravasio, S.; Dossena, L.; Martin-Figueroa, E.; Florencio, F.J.; Mattevi, A.; Morandi, P.; Curti, B.; Vanoni, M.A.
Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit
Biochemistry
41
8120-8133
2002
Azospirillum brasilense
brenda
Agnelli, P.; Dossena, L.; Colombi, P.; Mulazzi, S.; Morandi, P.; Tedeschi, G.; Negri, A.; Curti, B.; Vanoni, M.A.
The unexpected structural role of glutamate synthase [4Fe-4S](+1,+2) clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme beta subunit
Arch. Biochem. Biophys.
436
355-366
2005
Azospirillum brasilense
brenda
Stutz, H.E.; Reid, S.J.
GltX from Clostridium saccharobutylicum NCP262: glutamate synthase or oxidoreductase?
Biochim. Biophys. Acta
1676
71-82
2004
Clostridium saccharobutylicum (Q841S7), Clostridium saccharobutylicum NCP262 (Q841S7)
brenda
Petoukhov, M.V.; Svergun, D.I.; Konarev, P.V.; Ravasio, S.; van den Heuvel, R.H.; Curti, B.; Vanoni, M.A.
Quaternary structure of Azospirillum brasilense NADPH-dependent glutamate synthase in solution as revealed by synchrotron radiation x-ray scattering
J. Biol. Chem.
278
29933-29939
2003
Azospirillum brasilense (Q05755), Azospirillum brasilense
brenda
Coiro, V.M.; Di Nola, A.; Vanoni, M.A.; Aschi, M.; Coda, A.; Curti, B.; Roccatano, D.
Molecular dynamics simulation of the interaction between the complex iron-sulfur flavoprotein glutamate synthase and its substrates
Protein Sci.
13
2979-2991
2004
Azospirillum brasilense
brenda
Saum, S.H.; Sydow, J.F.; Palm, P.; Pfeiffer, F.; Oesterhelt, D.; Mueller, V.
Biochemical and molecular characterization of the biosynthesis of glutamine and glutamate, two major compatible solutes in the moderately halophilic bacterium Halobacillus halophilus
J. Bacteriol.
188
6808-6815
2006
Halobacillus halophilus (Q0E5H3), Halobacillus halophilus (Q0E5H4), Halobacillus halophilus (Q0E5H5), Halobacillus halophilus
brenda
Chung, T.W.; Lee, D.I.; Kim, D.S.; Jin, U.H.; Park, C.; Kim, J.G.; Kim, M.G.; Ha, S.D.; Kim, K.S.; Lee, K.H.; Kim, K.Y.; Chung, D.H.; Kim, C.H.
Molecular cloning and characterization of a large subunit of Salmonella typhimurium glutamate synthase (GOGAT) gene in Escherichia coli
J. Microbiol.
44
301-310
2006
Salmonella enterica subsp. enterica serovar Typhimurium (Q9L694), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Suzuki, A.; Knaff, D.B.
Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism
Photosynth. Res.
83
191-217
2005
Klebsiella aerogenes, Priestia megaterium, no activity in Arabidopsis thaliana, Pyrococcus sp., Rhodospirillum rubrum, Methanococcus thermoautotrophicum (O26308), Archaeoglobus fulgidus (O29309), Escherichia coli (P09831), Escherichia coli (P09832), Bacillus subtilis (P39812), Pseudomonas aeruginosa (P95456), Pseudomonas aeruginosa (P95457), Azospirillum brasilense (Q05755), Azospirillum brasilense (Q05756), Azospirillum brasilense (Q59084), Acidithiobacillus ferrooxidans (Q56266), Acidithiobacillus ferrooxidans (Q56267), Methanocaldococcus jannaschii (Q58746), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZLR3), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZLR4), Rhizobium etli (Q9ZFB8), Rhizobium etli (Q9ZFB9), Pyrococcus sp. KOD1
brenda
Vanoni, M.A.; Dossena, L.; van den Heuvel, R.H.; Curti, B.
Structure-function studies on the complex iron-sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation
Photosynth. Res.
83
219-238
2005
Azospirillum brasilense
brenda
Hemmilä, I.A.; Mäntsälä, P.I.
Inactivation of glutamate dehydrogenase and glutamate synthase from Bacillus megaterium by phenylglyoxal, butane-2,3-dione and pyridoxal 5'-phosphate
Biochem. J.
173
53-58
1978
Priestia megaterium
brenda
Cottevieille, M.; Larquet, E.; Jonic, S.; Petoukhov, M.V.; Caprini, G.; Paravisi, S.; Svergun, D.I.; Vanoni, M.A.; Boisset, N.
The subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: functional implications
J. Biol. Chem.
283
8237-8249
2008
Azospirillum brasilense (Q05756)
brenda
Jeelani, G.; Husain, A.; Sato, D.; Ali, V.; Suematsu, M.; Soga, T.; Nozaki, T.
Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica
J. Biol. Chem.
285
26889-26899
2010
Entamoeba histolytica (C4LUA1), Entamoeba histolytica (C8KIP3), Entamoeba histolytica, Entamoeba histolytica HM1:IMSS cl 6 (C4LUA1), Entamoeba histolytica HM1:IMSS cl 6 (C8KIP3)
brenda
Dincturk, H.B.; Cunin, R.; Akce, H.
Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii
Microbiol. Res.
166
294-303
2011
Pyrococcus horikoshii (A0A171), Pyrococcus horikoshii (B3FYT6), Pyrococcus horikoshii
brenda
Dincturk, H.; Cunin, R.; Akce, H.
Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii
Microbiol. Res.
166
294-303
2011
Pyrococcus horikoshii (O58606), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58606), Pyrococcus horikoshii OT3 (O59547)
brenda
Swuec, P.; Chaves-Sanjuan, A.; Camilloni, C.; Vanoni, M.A.; Bolognesi, M.
Cryo-EM structures of Azospirillum brasilense glutamate synthase in its oligomeric assemblies
J. Mol. Biol.
431
4523-4526
2019
Azospirillum brasilense (Q05755 and Q05756), Azospirillum brasilense
brenda