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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). The reaction takes place in the direction of L-glutamate production. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.2, glutamate dehydrogenase).
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
2
+
=
+
+
+
Synonyms
nadh-gogat, glutamate synthetase, nadh-dependent glutamate synthase, nadh-glutamate synthase, nadh-gogat1, nadh-gogat2, nadh-glts, glta2, gogat1, nadh-gogat i, 
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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
L-glutamate + NAD+ + H2O = NH3 + 2-oxoglutarate + NADH + H+
(1b)
-
-
-
L-glutamate + NH3 = L-glutamine + H2O
(1a)
-
-
-
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
kinetic mechanism
-
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
overall reaction
-
-
-
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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). The reaction takes place in the direction of L-glutamate production. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.2, glutamate dehydrogenase).
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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+
-
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+
-
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+
-
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+
-
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+
-
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+
-
-
-
?
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+
-
-
-
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+
-
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
-
?