HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.4.1.14 - glutamate synthase (NADH)
for references in articles please use BRENDA:EC1.4.1.14
Word Map on EC 1.4.1.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.4.1.14
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
glutamate synthase (NADH)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
transamidation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (transaminating)
A flavoprotein (FMN).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
65589-88-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isozymes encoded by genes gltA and gltA2 of the gltAB operon
-
-
cv. Xanthi, transgenic tobacco that overexpress NADH-GOGAT from Medicago sativa, higher capacity to assimilate nitrogen due to a higher NADH-GOGAT activity
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
-
NADH-GOGAT occurrs at higher levels in young and nonexpanded leaves and decreases with leaf age
-
low concentrations, but 15-40% higher enzyme activity in the roots of transgenic plants than of control plants
-
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
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
-
high enzyme activity in nodules compared to roots and other organs
-
enzyme activity increases markedly during development of effective root nodules
-
NADH-GOGAT II is twice as active as NADH-GOGAT I in mature nodules
-
NADH-GOGAT-II expression is higher than NADH-GOGAT-I during nodule development
additional information
organ specific expression pattern analysis
additional information
-
little or no enzyme activity and mRNA in leaves, stems, cotyledons and roots
additional information
-
enzyme is translated in sclerenchyma cells and transported to the root surface through epidermal and exodermal cells
additional information
-
not found in crude soluble protein fractions from leaves or bacteroids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
major portion of enzyme activity resides in the plastidial fraction
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50% glycerol, 100 mM potassium phosphate, 3 mM DTT, stable for up to 1 month
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes: NADH-GOGAT I with 877fold purification and NADH-GOGAT II with 631fold purification
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.4.1.14)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
