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Information on EC 1.4.1.14 - glutamate synthase (NADH)
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1.4.1.14 glutamate synthase (NADH)IUBMB Comments
A flavoprotein (FMN).
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
nadh-gogat, glutamate synthetase, nadh-dependent glutamate synthase, nadh-glutamate synthase, nadh-gogat1, nadh-gogat2, glta2, nadh-gogat i, nadh-gogat ii, glutamine 2-oxoglutarate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gltA
GltA2
gltB
-
large subunit of the glutamate synthase, plays a key role in Burkholderia vietnamiensis ability at growing in nitrogen-free media
glutamate (reduced nicotinamide adenine dinucleotide) synthase
-
-
-
-
glutamate synthase
-
-
-
-
glutamate synthase (NADH)
-
-
-
-
glutamate synthase (NADH-dependent)
-
-
-
-
glutamate synthetase
-
-
-
-
GOGAT
L-glutamate synthase (NADH)
-
-
-
-
L-glutamate synthetase
-
-
-
-
NADH-dependent glutamate synthase
NADH-GltS
NADH-glutamate synthase
NADH-GOGAT
NADH: GOGAT
-
-
-
-
synthase, glutamate (reduced nicotinamide adenine dinucleotide)
-
-
-
-
NADH-dependent glutamate synthase
-
-
-
-
NADH-GltS
-
-
-
-
NADH-glutamate synthase
-
-
-
-
NADH-GOGAT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
kinetic mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
transamidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (transaminating)
A flavoprotein (FMN).
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CAS REGISTRY NUMBER
COMMENTARY
65589-88-0
-
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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
L-glutamine + 2-oxoglutarate + reduced form of 3-acetylpyridine adenine dinucleotide
L-glutamine + oxidized form of 3-acetylpyridine adenine dinucleotide
-
reduced form of 3-acetylpyridine adenine dinucleotide is an alternative reductant to NADH, binds as tightly as NADH, enzyme catalyzes NADH-dependent reduction of AcPdAD+ by a substituted-enzyme ping-pong mechanism
-
?
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
r
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme for glutamate production
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme for glutamate production
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
regulatory role in biosynthesis pathways involving glutamate, early acceptor of fixed nitrogen
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation from fixed nitrogen, de novo synthesis of glutamate
-
-
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
role in overall ammonia assimilation system, involved in nitrogen metabolism
-
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids
-
-
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
root nodule ammonia assimilation, enzyme plays a central role in the functioning of effective root nodules
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
predominant enzyme in N2-fixing root nodules and roots, whereas in leaves and cotyledons Fd-GOGAT is the major form of GOGAT involved in nitrogen assimilation, NADH-GOGAT may be a rate-limiting step in NH4+ assimilation in root nodules
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
plays a critical role in the assimilation of symbiotically fixed nitrogen in nodules and during pollen development
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
important role in glutamine degradation
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
Neurospora crassa am-1
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamate biosynthesis
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
assimilation of exogeneously supplied NH4+ is primarily via the cytosolic glutamine synthetase/plastidial NADH-GOGAT cycle in specific regions of the epidermis and exodermis in roots
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
important role in the generation of glutamate for the assimilation of ammonium ions via the glutamine synthetase reaction in the epidermis and exodermis of the root surface, role in the re-utilization of glutamine transported from phloem and xylem in young leaves and grains at the early stage of ripening of rice plants
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
important role in the generation of glutamate for the assimilation of ammonium ions via the glutamine synthetase reaction in the epidermis and exodermis of the root surface, role in the re-utilization of glutamine transported from phloem and xylem in young leaves and grains at the early stage of ripening of rice plants
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
role in synthesis of glutamate for growth and development in higher plants
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
enzyme in developing organs, such as unexpanded non-green leaves and developing grains, could be involved in the utilization of remobilized nitrogen
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamate biosynthesis
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamate biosynthesis
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
involvement in glutamine metabolism, when glucose is in excess
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
involvement in glutamine metabolism, when glucose is in excess
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
1 mol 2-oxoglutarate and 1 mol glutamine are consumed per mol NADH oxidized
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
absolute specificity for 2-oxoglutarate
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
absolute specificity for 2-oxoglutarate
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
absolute specificity for 2-oxoglutarate
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
NADH binds first before enzyme is capable to bind other substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
absolute substrate specificity
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
1 mol 2-oxoglutarate and 1 mol glutamine are consumed per mol NADH oxidized
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
2-oxoglutarate may bind first and then L-glutamine, binding steps of NADH and 2-oxoglutarate are independent and random in order, or the mechanism may be ping-pong
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
mechanism involves compulsory, very tightly binding of NADH as first substrate, followed by random-order binding of glutamine and 2-oxoglutarate, NADH triggers a conformational change, which then exposes the binding sites of the other substrates
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
NADH-GOGAT transferrs [5-15N] of Gln to [2-15N]-Glu as soon as 10 min after [15N]ammonium feeding in the light, while the [2-15N]Glu labeling by GOGAT is slightly delayed in darkness
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
low activity when NH3 is substituted for glutamine, NH4Cl: 2.7% of the activity with L-glutamine
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
low activity when NH3 is substituted for glutamine, NH4Cl: 2.7% of the activity with L-glutamine
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
highly specific for its substrates
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
specific for NADH
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
additional information
?
-
-
no activity with L-asparagine, NH4Cl, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with hydroxylamine
-
-
-
additional information
?
-
-
no activity with L-asparagine, NH4Cl, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with L-asparagine, NH4Cl, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with albizziin, 6-diazo-5-oxo-L-norvaline, azaserine, methionine sulfoximine, FADH or FMNH
-
-
-
additional information
?
-
-
no activity with L-asparagine, NH4Cl, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with L-asparagine, NH4Cl, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with L-asparagine, ammonium sulfate, 2-oxobutyrate, oxaloacetate
-
-
-
additional information
?
-
-
sodium dithionite is no alternative reductant
-
-
-
additional information
?
-
-
enzyme is important for nitrogen assimilation, reduced enzyme ativity impairs N assimilation, overview
-
-
-
additional information
?
-
-
no activity with L-asparagine, NH4Cl or NADPH
-
-
-
additional information
?
-
-
no activity with L-asparagine, NH4Cl, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with L-asparagine, D-glutamine, pyruvate, oxaloacetate or NADPH
-
-
-
additional information
?
-
-
no activity with 2-oxovalerate, 2-oxopimelate, 2-oxoadipate, oxaloacetate, D-glutamine, L- or D-asparagine, L- or D-homoglutamine, alpha-methyl-L-glutamine, DL-beta-glutamine, L-isoglutamine, glutaramide or glutaramate
-
-
-
additional information
?
-
-
no activity with 2-oxovalerate, 2-oxopimelate, 2-oxoadipate, oxaloacetate, D-glutamine, L- or D-asparagine, L- or D-homoglutamine, alpha-methyl-L-glutamine, DL-beta-glutamine, L-isoglutamine, glutaramide or glutaramate
-
-
-
additional information
?
-
-
no activity with L-asparagine, D-glutamine, pyruvate, oxaloacetate or NADPH
-
-
-
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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
additional information
?
-
-
enzyme is important for nitrogen assimilation, reduced enzyme ativity impairs N assimilation, overview
-
-
-
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
B9FLJ1, Q0JKD0
-
-
-
r
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
r
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme for glutamate production
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme for glutamate production
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
regulatory role in biosynthesis pathways involving glutamate, early acceptor of fixed nitrogen
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation from fixed nitrogen, de novo synthesis of glutamate
-
-
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
role in overall ammonia assimilation system, involved in nitrogen metabolism
-
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids
-
-
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
root nodule ammonia assimilation, enzyme plays a central role in the functioning of effective root nodules
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
predominant enzyme in N2-fixing root nodules and roots, whereas in leaves and cotyledons Fd-GOGAT is the major form of GOGAT involved in nitrogen assimilation, NADH-GOGAT may be a rate-limiting step in NH4+ assimilation in root nodules
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
plays a critical role in the assimilation of symbiotically fixed nitrogen in nodules and during pollen development
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
important role in glutamine degradation
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
Neurospora crassa am-1
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamate biosynthesis
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
assimilation of exogeneously supplied NH4+ is primarily via the cytosolic glutamine synthetase/plastidial NADH-GOGAT cycle in specific regions of the epidermis and exodermis in roots
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
important role in the generation of glutamate for the assimilation of ammonium ions via the glutamine synthetase reaction in the epidermis and exodermis of the root surface, role in the re-utilization of glutamine transported from phloem and xylem in young leaves and grains at the early stage of ripening of rice plants
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
important role in the generation of glutamate for the assimilation of ammonium ions via the glutamine synthetase reaction in the epidermis and exodermis of the root surface, role in the re-utilization of glutamine transported from phloem and xylem in young leaves and grains at the early stage of ripening of rice plants
one of the two synthezised glutamate molecules can be cycled back as substrate for glutamine synthetase reaction and the other can be used for many synthetic reactions
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
role in synthesis of glutamate for growth and development in higher plants
-
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
enzyme in developing organs, such as unexpanded non-green leaves and developing grains, could be involved in the utilization of remobilized nitrogen
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
ammonia assimilation
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamate biosynthesis
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
glutamate biosynthesis
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
involvement in glutamine metabolism, when glucose is in excess
-
ir
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
involvement in glutamine metabolism, when glucose is in excess
-
ir
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
reduced form is an alternative reductant, binds as tightly as NADH
FMN
-
coding region important for binding of flavin mononucleotide is located on exon 16
NADH
-
exclusively dependent on NADH as coenzyme; specific for NADH as reductant
NADH
-
five conserved residues important for NADH binding are located in exon 20
additional information
-
absence of flavin and iron; no activity with NADPH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3Fe-4S-center
Mg2+
additional information
3Fe-4S-center
-
flavoprotein containing an iron-sulfur cluster: 3Fe-4S cluster
additional information
C-terminal binding domain for a 3Fe-4S cluster
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,5-dioxoimidazolidin-4-yl)urea
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM allantoine
2-Hydroxyglutarate
-
D- and L-isomer, most potent competitive inhibitor
3-acetylpyridine adenine dinucleotide
-
competitive inhibitor with respect to NADH
allopurinol
-
activity of NADH-GOGAT I significantly decreases in the presence of 2 mM allopurinol
glutamine
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM glutamine
L-2-Amino-4-oxo-5-chloropentanoate
-
1 mM, 30 min, 0°C, pH 7.6, irreversible inhibition
L-homocysteine sulfonamide
-
very potent transition state inhibitor, competitive to L-glutamine
O-diazoacetyl-L-serine
-
1 mM, 30 min, 0°C, pH 7.6, irreversible inhibition
oxaloacetate
-
weak inhibition, competitive with 2-oxoglutarate
p-hydroxymercuribenzoate
-
complete inhibition at 0.1-1 mM, at 0.0005 mM 33% inhibition or 75% inhibition after preincubation in presence of glutamine and 2-oxoglutarate, substrates induce a conformation, which makes essential sulfhydryl groups more accessible to reagent
xanthine
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM xanthine
(2S)-2-amino-4-(S-methylsulfonimidoyl)butanoic acid
-
potent irreversible inhibitor
6-diazo-5-oxo-L-norleucine
-
0.1 mM, 30 min, 0°C, pH 7.6, irreversible inhibition
asparagine
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM asparagine
glycine
-
48% inhibition at 10 mM, complete inhibition at 20 mM
L-Albizziin
-
less inhibitory than L-homocysteine sulfonamide, methionine sulfone and ethionine sulfone
L-glutamate
-
competitive with 2-oxoglutarate; glutamate binds 1.7times more tightly in the presence of NAD+
tryptophan
-
29% inhibition at 10 mM, complete inhibition at 20 mM
additional information
-
not inhibited by 1 mM cyanide or cyanate
-
additional information
-
cumulative inhibition by combinations of amino acids and nucleotides, cumulative feedback inhibition
-
additional information
-
not inhibited by alanine, glycine, serine, lysine, proline, cysteine, valine, leucine, isoleucine, threonine, phenylalanine, histidine, tryptophan, asparagine, arginine, UTP, ITP, GTP
-
additional information
-
not inhibited by 2,2’-dipyridyl or N-ethylmaleimide
-
additional information
-
the presence of asparagine, glutamine, xanthine, allantoin, allopurinol in the nutrient solution does not affect the expression of NADH-GOGAT-II in the nodules
-
additional information
-
not inhibited by the 20 common amino acids at a concentration of 20 mM
-
additional information
-
enzyme activity declines significantly between 42-68% and 9-42% relative water content in leaves
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1%, presence of a reducing agent is essential for enzyme activity
diphosphate
-
5 mM, stimulates activity with 36% enhancement
dithiothreitol
-
0.5 mg per ml, presence of a reducing agent is essential for enzyme activity
GltB
-
GltA and not GltA2 is dependent on GltB for GOGAT activity in vivo
-
NH4Cl
-
NADH-GOGAT gene expression is transiently induced within a few hours of supplying either 1 or 25 mM to the medium, leading to a marked accumulation of NADH-GOGAT mRNA
NH4NO3
-
transcripts for NADH-GOGAT transiently accumulate when 0.5 mM is applied
additional information
-
not activated by pyridoxal 5’-phosphate and pyridoxamine 5’-phosphate
-
additional information
-
supply of NH4+ at low concentrations increases the expression of the enzyme: supply with 1 mM NH4+ for 24 h increases the enzyme content in the epidermis and exodermis of the root surface
-
additional information
-
NH4+ transiently induces accumulation of enzyme mRNA in roots of rice seedlings, maximally 3-6 h after supply
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
2-oxoglutarate
-
with reduced form of 3-acetylpyridine adenine dinucleotide as reductant
0.014
3-acetylpyridine adenine dinucleotide
-
NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide
0.125
L-glutamine
-
with reduced form of 3-acetylpyridine adenine dinucleotide as reductant
0.0014
NADH
-
NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
3-acetylpyridine adenine dinucleotide
-
reduced form as reductant, glutamate synthase reaction
51
3-acetylpyridine adenine dinucleotide
-
NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
additional information
additional information
-
enzyme specific activity of transformants is significantly greater than that of control plants
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
8.5
9
-
ammonia-dependent NADH oxidase activity, rate steadily increases from pH 6 to 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isozymes encoded by genes gltA and gltA2 of the gltAB operon
-
-
brenda
two isozymes encoded by genes gltA and gltA2 of the gltAB operon
-
-
brenda
cv. Xanthi, transgenic tobacco that overexpress NADH-GOGAT from Medicago sativa, higher capacity to assimilate nitrogen due to a higher NADH-GOGAT activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
shorter than 10 mm, supply with 1 mM ammonium ions for 24 h increases the enzyme content in the epidermis and exodermis cells of the root surface
brenda
additional information
-
NADH-GOGAT occurrs at higher levels in young and nonexpanded leaves and decreases with leaf age
brenda
-
low concentrations, but 15-40% higher enzyme activity in the roots of transgenic plants than of control plants
brenda
-
roots of seedlings: root tips and area where the secondary roots are actively developing, enzyme in the central cylinder, apical meristem and the primordia of secondary roots of seedlings grown for 26 d in water, supply with 1 mM ammonium ions for 24 h increases the enzyme content in the epidermis and exodermis of the root surface
brenda
NADH-GOGAT is primarily located in plastids of non-photosynthetic tissues such as roots; NADH-GOGAT is primarily located in plastids of non-photosynthetic tissues such as roots
brenda
-
high enzyme activity in nodules compared to roots and other organs
brenda
-
enzyme activity increases markedly during development of effective root nodules
brenda
-
NADH-GOGAT II is twice as active as NADH-GOGAT I in mature nodules
brenda
-
NADH-GOGAT-II expression is higher than NADH-GOGAT-I during nodule development
brenda
additional information
organ specific expression pattern analysis
brenda
additional information
-
little or no enzyme activity and mRNA in leaves, stems, cotyledons and roots
brenda
additional information
-
enzyme is translated in sclerenchyma cells and transported to the root surface through epidermal and exodermal cells
brenda
additional information
-
not found in crude soluble protein fractions from leaves or bacteroids
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
major portion of enzyme activity resides in the plastidial fraction
brenda
-
exclusively plastidial location, various forms of plastids in cells of epidermis and exodermis, in the cortex parenchyma and vascular parenchyma of root tips, epidermis and exodermis cells contain more plastids and much higher enzyme concentration than other root cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme disruption in Oidiodendron maius induces reorganization of the N pathway and reduces tolerance to heavy-metals like zinc
physiological function
physiological function
-
the glutamine synthetase-glutamate synthase cycle plays an important role for proline synthesis in tomato leaves during salinity stress, while NADH-dependent glutamate synthase (NADHGOGAT) activity is unchanged due to salinity stress
physiological function
-
isoform NADH-GOGAT1 is important in the primary assimilation of NH4+ taken up by rice roots, while isoform NADH-GOGAT2 is important in remobilization of nitrogen during natural senescence
physiological function
-
NADH-dependent glutamate synthase plays a key role in assimilating ammonium in the Arabidopsis root
physiological function
-
the glutamine synthetase-glutamate synthase cycle plays an important role for proline synthesis in tomato leaves during salinity stress, while NADH-dependent glutamate synthase (NADHGOGAT) activity is unchanged due to salinity stress
-
Show AA Sequence and Transmembrane Helices (622 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17500
-
2 * 91000 + 2 * 86000 + 2 * 68000 + 2 * 31000 + 2 * 17500, SDS-PAGE
31000
-
2 * 91000 + 2 * 86000 + 2 * 68000 + 2 * 31000 + 2 * 17500, SDS-PAGE
61000
-
1 * 169000 + 1 * 61000, SDS-PAGE in presence of 1% 2-mercaptoethanol
68000
-
2 * 91000 + 2 * 86000 + 2 * 68000 + 2 * 31000 + 2 * 17500, SDS-PAGE
86000
-
2 * 91000 + 2 * 86000 + 2 * 68000 + 2 * 31000 + 2 * 17500, SDS-PAGE
91000
-
2 * 91000 + 2 * 86000 + 2 * 68000 + 2 * 31000 + 2 * 17500, SDS-PAGE
169000
-
1 * 169000 + 1 * 61000, SDS-PAGE in presence of 1% 2-mercaptoethanol
200000
229000
-
calculated from the cDNA sequence, without N-terminal presequence of 101 amino acids
235000
240000
265000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
-
2 * 91000 + 2 * 86000 + 2 * 68000 + 2 * 31000 + 2 * 17500, SDS-PAGE
dimer
-
1 * 169000 + 1 * 61000, SDS-PAGE in presence of 1% 2-mercaptoethanol
monomer
additional information
-
protein contains domains that correspond to both the large alpha subunit with 46% identity and the small beta subunit with 38% identity of Escherichia coli NADPH-GOGAT, a 57 amino acid highly charged domain connects the two regions homologous to the prokaryotic subunits
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
enzyme is synthesized as proprotein with a N-terminal propeptide region
proteolytic modification
-
enzyme is synthesized as proprotein with a N-terminal propeptide region
proteolytic modification
-
primary translation product is a 240 kDa protein, that contains a N-terminal 101 amino acid presequence resulting in a processed protein of 229 kDa
proteolytic modification
-
translational gene product has a 99 amino acid presequence at the N-terminal region
proteolytic modification
-
enzyme is synthesized as proprotein with a N-terminal propeptide region
proteolytic modification
-
enzyme is synthesized as proprotein with a N-terminal propeptide region
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of the inactive knock-out T-DNA insertion mutant glt1-T, insertion between D315 and G316 of exon 9, mutant plants are specifically defective in growth and glutamate biosynthesis when photorespiration is repressed by 1% CO2, overview
additional information
-
GOGAT mutant 4B8 is found to grow onto nitrogen-free medium supplemented with 0.5% glutamate or 0.5% glutamine but not 5 mM NH4Cl, confirming the role of this enzyme in the assimilation of either ammonium derived from fixed and non-fixed nitrogen sources
additional information
-
GOGAT-deficient mutants show a growth defect under low NH4 conditions
additional information
-
construction of 4 transgenic alfalfa lines, i.e. GA89, GA87, GA88, and GA82, tranformed with an antisense enzyme cDNA fragment under control of the soybean leghemoglobin promotor lbc3, mutants show reduced enzyme activity and content in the nodules, altered chlorotic phenotypes, reduced fresh weight, and lower N-content compared to wild-type plants, overview
additional information
-
three en(am)-2 mutants, lacking enzyme activity, no growth on ammonia-limited conditions
additional information
suppression of the enzyme leads to significantly increased 2-oxoglutarate levels in leaves in most co-suppressed lines compared with the wild-type, in the leaf, the 2-oxoglutarate precursor, isocitrate, shows the same trend. The contents of oxaloacetate, malate, and pyruvate are also increased in some, but not all, co-suppressed lines. The mutants show altered chlorophyll contents, phenotypes, overview; suppression of the enzyme leads to significantly increased 2-oxoglutarate levels in leaves in most co-suppressed lines compared with the wild-type, in the leaf, the 2-oxoglutarate precursor, isocitrate, shows the same trend. The contents of oxaloacetate, malate, and pyruvate are also increased in some, but not all, co-suppressed lines. The mutants show altered chlorophyll contents, phenotypes, overview
additional information
suppression of the enzyme leads to significantly increased 2-oxoglutarate levels in leaves in most co-suppressed lines compared with the wild-type, in the leaf, the 2-oxoglutarate precursor, isocitrate, shows the same trend. The contents of oxaloacetate, malate, and pyruvate are also increased in some, but not all, co-suppressed lines. The mutants show altered chlorophyll contents, phenotypes, overview; suppression of the enzyme leads to significantly increased 2-oxoglutarate levels in leaves in most co-suppressed lines compared with the wild-type, in the leaf, the 2-oxoglutarate precursor, isocitrate, shows the same trend. The contents of oxaloacetate, malate, and pyruvate are also increased in some, but not all, co-suppressed lines. The mutants show altered chlorophyll contents, phenotypes, overview
additional information
-
GOGAT-deficient mutants show a growth defect under low NH4 conditions
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
-
half-life: 10 min, presence of 2-oxoglutarate and L-glutamine stabilizes against thermal denaturation, whereas preincubation with NADH or L-glutamate causes more heat sensitivity
additional information
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
2-oxoglutarate, 2-mercaptoethanol and EDTA stabilize and have a synergystic effect
-
EDTA stabilizes
highly labile enzyme activity
phenylmethylsulphonyl fluoride is used as precaution against proteolysis
phenylmethylsulphonyl fluoride is used as precaution against proteolysis
-
phenylmethylsulphonyl fluoride is used as precaution against proteolysis
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50% glycerol, 100 mM potassium phosphate, 3 mM DTT, stable for up to 1 month
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes: NADH-GOGAT I with 877fold purification and NADH-GOGAT II with 631fold purification
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene encoding NADH-GltS is cloned, N-terminal three quarters of the gene product is similar to the bacterial alpha subunit from NADPH-GltS
isolation and characterization of NADH-GOGAT gene with 22 exons and 21 introns, isolation of 7.2 kbp cDNA encoding the complete enzyme
-
locus of structural gene encoding NADH-GOGAT is mapped on chromosome 1, detection of quantitative trait loci associated with the enzyme content in leaves
-
NADH-GOGAT1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, relative real-time RT-PCR expression analysis; NADH-GOGAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, relative real-time RT-PCR expression analysis
open reading frames encoding proteins similar to NADH-GltS are found during sequencing of genome
overexpression of chimeric NADH-GOGAT gene from Medicago sativa fused to the CaMV 35S promoter in transgenic Nicotiana tabacum
-
transgenic plants expressing antisense Fd-GOGAT mRNA, NADH-GOGAT activity remains low
-
transgenic tobacco lines harboring the GLU1 promoter of the Arabidopsis Fd-GOGAT fused to a GUS reporter gene, NADH-GOGAT activity decreases in old leaves by 32% to 35%
-
gene encoding NADH-GltS is cloned, N-terminal three quarters of the gene product is similar to the bacterial alpha subunit from NADPH-GltS
-
gene encoding NADH-GltS is cloned, N-terminal three quarters of the gene product is similar to the bacterial alpha subunit from NADPH-GltS
-
open reading frames encoding proteins similar to NADH-GltS are found during sequencing of genome
-
open reading frames encoding proteins similar to NADH-GltS are found during sequencing of genome
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
possible relationship between NADH-GOGAT, IDH and GDH, IDH is a good candidate to generate the 2-oxoglutarate required for NH4+-induced NADH-GOGAT activity in rice roots, GDH shows no significant differences in its localization between the conditions with or without NH4+ application
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meister, A.
Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae
Methods Enzymol.
113
327-337
1985
Saccharomyces cerevisiae
brenda
Boland, M.J.; Benny, A.G.
Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules
Eur. J. Biochem.
79
355-362
1977
Lupinus angustifolius
brenda
Hayakawa, T.; Yamaya, T.; Kamachi, K.; Ojima, K.
Purification, characterization, and immunological properties of NADH-dependent glutamate synthase from rice cell cultures
Plant Physiol.
98
1317-1322
1992
Oryza sativa
brenda
Anderson, M.P.; Vance, C.P.; Heichel, G.H.; Miller, S.S.
Purification and characterization of NADH-glutamate synthase from alfalfa root nodules
Plant Physiol.
90
351-358
1989
Medicago sativa
brenda
Chen, F.L.; Cullimore, J.V.
Two isoenzymes of NADH-dependent glutamate synthase in root nodules of Phaseolus vulgaris L.. Purification, properties and activity changes during nodule development
Plant Physiol.
88
1411-1417
1988
Phaseolus vulgaris
brenda
Singhal, R.K.; Krishnan, I.S.; Dua, R.D.
Stabilization, purification, and characterization of glutamate synthase from Clostridium pasteurianum
Biochemistry
28
7928-7935
1989
Clostridium pasteurianum
brenda
Masters, D.S.; Meister, A.
Inhibition by homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae
J. Biol. Chem.
257
8711-8715
1982
Saccharomyces cerevisiae
brenda
Romero, D.; Davila, G.
Genetic and biochemical identification of the glutamate synthase structural gene in Neurospora crassa
J. Bacteriol.
167
1043-1047
1986
Neurospora crassa
brenda
Wang, R.; Nicholas, D.J.D.
Some properties of glutamine synthetase and glutamate synthase from Derxia gummosa
Phytochemistry
24
1133-1139
1985
Derxia gummosa
-
brenda
Khanna, S.; Nicholas, D.J.D.
Some properties of glutamine synthetase and glutamate synthase from Chlorobium vibrioforme f. thiosulfatophilum
Arch. Microbiol.
134
98-103
1983
Chlorobium vibrioforme f. thiosulfatophilum, Chlorobium vibrioforme f. thiosulfatophilum NCIB 8346
-
brenda
Boland, M.J.; Court, C.B.
Glutamate synthase (NADH) from lupin nodules. Specificity of the 2-oxoglutarate site
Biochim. Biophys. Acta
657
539-542
1981
Lupinus angustifolius
brenda
Hummelt, G.; Mora, J.
NADH-dependent glutamate synthase and nitrogen metabolism in Neurospora crassa
Biochem. Biophys. Res. Commun.
92
127-133
1980
Neurospora crassa, Neurospora crassa am-1
brenda
Miyatake, K.; Kitaoka, S.
NADH-dependent glutamate synthase in Euglena gracilis z
Agric. Biol. Chem.
45
1727-1729
1981
Euglena gracilis, Euglena gracilis Z
brenda
Boland, M.J.
NADH-dependent glutamate synthase from lupin nodules. Reactions with oxidised and reduced 3-acetylpyridine-adenine dinucleotide
Eur. J. Biochem.
115
485-489
1981
Lupinus angustifolius
brenda
Marquez, A.J.; Galvan, F.; Vega, J.M.
Purification and characterization of the NADH-glutamate synthase from Chlamydomonas reinhardii
Plant Sci. Lett.
34
305-314
1984
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 21 gr
-
brenda
Roon, R.J.; Even, H.I.; Larimore, F.
Glutamate synthase: Properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae
J. Bacteriol.
118
89-95
1974
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180A
brenda
Boland, M.J.
Kinetic mechanism of NADH-dependent glutamate synthase from lupin nodules
Eur. J. Biochem.
99
531-539
1979
Lupinus angustifolius
brenda
Cordovilla, M.P.; Perez, J.; Ligero, F.; Lluch, C.; Valpuesta, V.
Partial purification and characterization of NADH-glutamate synthase from faba bean (Vicia faba) root nodules
Plant Sci.
150
121-128
2000
Vicia faba
-
brenda
Ishiyama, K.; Hayakawa, T.; Yamaya, T.
Expression of NADH-dependent glutamate synthase protein in the epidermis and exodermis of rice roots in response to the supply of ammonium ions
Planta
204
288-294
1998
Oryza sativa
brenda
Hayakawa, T.; Hopkins, L.; Peat, L.J.; Yamaya, T.; Tobin, A.K.
Quantitative intercellular localization of NADH-dependent glutamate synthase protein in different types of root cells in rice plants
Plant Physiol.
119
409-416
1999
Oryza sativa
brenda
Obara, M.; Kajiura, M.; Fukuta, Y.; Yano, M.; Hayashi, M.; Yamaya, T.; Sato, T.
Mapping of QTLs associated with cytosolic glutamine synthetase and NADH-glutamate synthase in rice (Oriza sativa L.)
J. Exp. Bot.
52
1209-1217
2001
Oryza sativa
brenda
Doverskog, M.; Jacobsson, U.; Chapman, B.E.; Kuchel, P.W.; Häggström, L.
Determination of NADH-dependent glutamate synthase (GOGAT) in Spodoptera frugiperda (Sf9) insect cells by a selective 1H/15N NMR in vitro assay
J. Biotechnol.
79
87-97
2000
Bombyx mori, Spodoptera frugiperda, Spodoptera frugiperda Sf9
brenda
Vanoni, M.A.; Curti, B.
Glutamate synthase: A complex iron-sulfur flavoprotein
Cell. Mol. Life Sci.
55
617-638
1999
Bombyx mori, Caenorhabditis elegans, Medicago sativa, Plasmodium falciparum, Saccharomyces cerevisiae
brenda
Vance, C.P.; Miller, S.S.; Gregerson, D.L.; Samac, D.A.; Robinson, D.L.; Gantt, J.S.
Alfalfa NADH-dependent glutamate synthase: Structure of the gene and importance in symbiotic N2 fixation
Plant J.
8
345-358
1995
Medicago sativa
brenda
Chichkova, S.; Arellano, J.; Vance, C.P.; Hernandez, G.
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Oryza sativa
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Localization of NAD-isocitrate dehydrogenase and glutamate dehydrogenase in rice roots: candidates for providing carbon skeletons to NADH-glutamate synthase
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Expression of a ferredoxin-dependent glutamate synthase gene in mesophyll and vascular cells and functions of the enzyme in ammonium assimilation in Nicotiana tabacum (L.)
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Nicotiana tabacum
brenda
Chao, L.; Bofu, P.; Weiqian, C.; Yun, L.; Hao, H.; Liang, C.; Xiaoqing, L.; Xiao, W.; Fashui, H.
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Valadier, M.H.; Yoshida, A.; Grandjean, O.; Morin, H.; Kronenberger, J.; Boutet, S.; Raballand, A.; Hase, T.; Yoneyama, T.; Suzuki, A.
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brenda
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Structure-function studies of glutamate synthases: a class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation
IUBMB Life
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Aedes aegypti, Anopheles gambiae, Bombyx mori, Caenorhabditis elegans, Ciona intestinalis, Drosophila melanogaster, Plasmodium falciparum
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Whittaker, A.; Martinelli, T.; Farrant, J.M.; Bochicchio, A.; Vazzana, C.
Sucrose phosphate synthase activity and the co-ordination of carbon partitioning during sucrose and amino acid accumulation in desiccation-tolerant leaf material of the C4 resurrection plant Sporobolus stapfianus during dehydration
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Molecular cloning, characterization and regulation of two different NADH-glutamate synthase cDNAs in bean nodules
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Phaseolus vulgaris
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brenda
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Protection of the glutamate pool concentration in enteric bacteria
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Escherichia coli, Salmonella enterica
brenda
Hayakawa, T.; Ishiyama, K.; Yamaya, T.
Tissue and cellular localization of NADH-dependent glutamate synthase protein in leaves of spinach
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Functional characterization of key enzymes involved in L-glutamate synthesis and degradation in the thermotolerant and methylotrophic bacterium Bacillus methanolicus
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Bacillus methanolicus, Bacillus methanolicus ATCC 53907
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Hossain, M.; Uddin, M.; Ismail, M.; Ashrafuzzaman, M.
Responses of glutamine synthetase-glutamate synthase cycle enzymes in tomato leaves under salinity stress
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Solanum lycopersicum, Solanum lycopersicum BINATomato-5
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SLu, Y.; Luo, F.; Yang, M.; Li, X.; Lian, X.
Suppression of glutamate synthase genes significantly affects carbon and nitrogen metabolism in rice (Oryza sativa L.)
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Oryza sativa Japonica Group (B9FLJ1), Oryza sativa Japonica Group (Q0JKD0)
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Khouja, H.; Daghino, S.; Abbà, S.; Boutaraa, F.; Chalot, M.; Blaudez, D.; Martino, E.; Perotto, S.
OmGOGAT-disruption in the ericoid mycorrhizal fungus Oidiodendron maius induces reorganization of the N pathway and reduces tolerance to heavy-metals
Fungal Genet. Biol.
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Oidiodendron maius
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Yamaya, T.; Kusano, M.
Evidence supporting distinct functions of three cytosolic glutamine synthetases and two NADH-glutamate synthases in rice
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Oryza sativa
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Konishi, N.; Ishiyama, K.; Matsuoka, K.; Maru, I.; Hayakawa, T.; Yamaya, T.; Kojima, S.
NADH-dependent glutamate synthase plays a crucial role in assimilating ammonium in the Arabidopsis root
Physiol. Plant.
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Arabidopsis thaliana
brenda
Kojima, S.; Konishi, N.; Beier, M.P.; Ishiyama, K.; Maru, I.; Hayakawa, T.; Yamaya, T.
NADH-dependent glutamate synthase participated in ammonium assimilation in Arabidopsis root
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Arabidopsis thaliana
brenda
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