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2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
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
-
?
additional information
?
-
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
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+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
-
-
?
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+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
ir
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+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
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+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
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+
-
specific for NADH
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
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+
-
-
-
-
ir
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
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
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
additional information
?
-
-
no activity with hydroxylamine
-
-
?
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
?
-
-
-
-
-
?
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.
2 L-glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
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
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+
-
glutamine synthetase/glutamate synthase pathway for ammonia assimilation is fafavoured by growth at low concentrations of ammonia
-
?
L-glutamine + 2-oxoglutarate + NADH
glutamate + NAD+
-
-
-
?
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 + H+
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
L-glutamine + 2-oxoglutarate + NADH + H+
L-glutamate + NAD+
-
-
-
-
?
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(2,5-dioxoimidazolidin-4-yl)urea
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM allantoine
(2S)-2-amino-4-(S-methylsulfonimidoyl)butanoic acid
2-hydroxyglutarate
-
D- and L-isomer, most potent competitive inhibitor
3-acetylpyridine adenine dinucleotide
-
competitive inhibitor with respect to NADH
6-diazo-5-oxo-L-norleucine
acridine
-
inhibitor of flavoenzymes, 65% inhibition
alanine
-
slight inhibition
allopurinol
-
activity of NADH-GOGAT I significantly decreases in the presence of 2 mM allopurinol
arginine
-
20 mM, complete inhibition
bathophenanthroline
-
50% inhibition
Cd2+
-
0.5 mM slightly decreases GOGAT activity in the absence of 2-oxoglutarate
citrate
-
inhibited by high concentrations, 40 mM
Cu2+
-
Cu2+ and Fe2+ are most inhibitory metal ions
D-glutamate
-
competitive inhibitor
Fe2+
-
Cu2+ and Fe2+ are most inhibitory metal ions
glutamine
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM glutamine
Glutarate
-
most potent competitive inhibitor
L-2-Amino-4-oxo-5-chloropentanoate
-
1 mM, 30 min, 0°C, pH 7.6, irreversible inhibition
L-histidine
-
25 mM, 20-30% inhibition
L-homocysteine sulfonamide
-
very potent transition state inhibitor, competitive to L-glutamine
L-methionine D,L-sulfoximine
-
-
L-methionine-SR-sulfoxide
leucine
-
10 mM, 52% inhibition
NADH
-
substrate inhibition at high concentrations
NADP+
-
1 mM, 48% inhibition
NADPH
-
0.2 mM, 50% inhibition
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
phenylalanine
-
20 mM, complete inhibition
Sodium dithionite
-
strong inhibitory effect
xanthine
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM xanthine
(2S)-2-amino-4-(S-methylsulfonimidoyl)butanoic acid
-
-
(2S)-2-amino-4-(S-methylsulfonimidoyl)butanoic acid
-
potent irreversible inhibitor
6-diazo-5-oxo-L-norleucine
-
76% inhibition at 5 mM
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
0.1 mM, 30 min, 0°C, pH 7.6, irreversible inhibition
ADP
-
10 mM, 84% inhibition
ADP
-
20 mM, about 75% inhibition
AMP
-
10 mM, 61% inhibition
AMP
-
20 mM, about 75% inhibition
asparagine
-
slight inhibition
asparagine
-
weak inhibition, competitive with 2-oxoglutarate
asparagine
-
activity of NADH-GOGAT I significantly decreases in the presence of 10 mM asparagine
aspartate
-
10 mM, 60% inhibition
aspartate
-
weak inhibition, competitive with 2-oxoglutarate
ATP
-
10 mM, 37% inhibition
ATP
-
5 mM, 75% inhibition
azaserine
-
completely inhibited by 1 mM, glutamine analog
azaserine
-
75% inhibition at 5 mM
azaserine
-
completely inhibited by 1 mM, glutamine analog
azaserine
-
glutamine antagonist, completely inhibited by 10 mM
azaserine
-
complete inhibition
azaserine
-
completely inhibited by 4 mM
azaserine
-
completely inhibited by 0.4 mM
azaserine
-
completely inhibited by 1 mM, glutamine analog
D-glutamine
-
-
D-glutamine
-
slight inhibition
DL-ethionine sulfone
-
-
DL-ethionine sulfone
-
potent competitive inhibitor
glycine
-
slight inhibition
glycine
-
48% inhibition at 10 mM, complete inhibition at 20 mM
L-Albizziin
-
-
L-Albizziin
-
less inhibitory than L-homocysteine sulfonamide, methionine sulfone and ethionine sulfone
L-glutamate
-
4 mM, 20% inhibition, product inhibition
L-glutamate
-
10 mM, 24% inhibition
L-glutamate
-
competitive with 2-oxoglutarate
L-glutamate
-
competitive with 2-oxoglutarate; glutamate binds 1.7times more tightly in the presence of NAD+
L-methionine sulfone
-
markedly inhibits
L-methionine sulfone
-
very potent competitive inhibitor
L-methionine-SR-sulfoxide
-
-
L-methionine-SR-sulfoxide
-
slight inhibition
malate
-
inhibited by high concentrations, 40 mM
malate
-
20 mM, 30% inhibition
methionine
-
25 mM L-methionine, 20-30% inhibition
methionine
-
10 mM, 47% inhibition
methionine
-
10 mM, 72% inhibition
NAD+
-
competitive with NADH
NAD+
-
1 mM, 27% inhibition
pyruvate
-
slight inhibition, analogue of 2-oxoglutarate
pyruvate
-
20 mM, 20% inhibition
serine
-
25 mM L-serine, 20-30% inhibition
serine
-
10 mM, 73% inhibition
tryptophan
-
25 mM L-tryptophan, 20-30% inhibition
tryptophan
-
29% inhibition at 10 mM, complete inhibition at 20 mM
additional information
-
not inhibited by 1 mM cyanide or cyanate
-
additional information
-
not inhibited by Mn2+ and Ca2+
-
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 vitamin B6-enzyme inhibitors
-
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
-
cumulative inhibition by combinations of amino acids and nucleotides, cumulative feedback inhibition
-
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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Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae
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Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules
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Lupinus angustifolius
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1989
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Two isoenzymes of NADH-dependent glutamate synthase in root nodules of Phaseolus vulgaris L.. Purification, properties and activity changes during nodule development
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1988
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Stabilization, purification, and characterization of glutamate synthase from Clostridium pasteurianum
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Inhibition by homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae
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Genetic and biochemical identification of the glutamate synthase structural gene in Neurospora crassa
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Neurospora crassa
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Some properties of glutamine synthetase and glutamate synthase from Derxia gummosa
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Derxia gummosa
-
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Some properties of glutamine synthetase and glutamate synthase from Chlorobium vibrioforme f. thiosulfatophilum
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1983
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-
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Glutamate synthase (NADH) from lupin nodules. Specificity of the 2-oxoglutarate site
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NADH-dependent glutamate synthase and nitrogen metabolism in Neurospora crassa
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NADH-dependent glutamate synthase in Euglena gracilis z
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1981
Euglena gracilis, Euglena gracilis Z
-
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NADH-dependent glutamate synthase from lupin nodules. Reactions with oxidised and reduced 3-acetylpyridine-adenine dinucleotide
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1981
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Purification and characterization of the NADH-glutamate synthase from Chlamydomonas reinhardii
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34
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1984
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 21 gr
-
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1974
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180A
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Lupinus angustifolius
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Partial purification and characterization of NADH-glutamate synthase from faba bean (Vicia faba) root nodules
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2000
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-
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Expression of NADH-dependent glutamate synthase protein in the epidermis and exodermis of rice roots in response to the supply of ammonium ions
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204
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Oryza sativa
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Quantitative intercellular localization of NADH-dependent glutamate synthase protein in different types of root cells in rice plants
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119
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Oryza sativa
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Occurrence of two forms of glutamate synthase in Chlamydomonas reinhardii
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Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CCAP 11/32A
-
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-
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-
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Responses of glutamine synthetase-glutamate synthase cycle enzymes in tomato leaves under salinity stress
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14
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-
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Suppression of glutamate synthase genes significantly affects carbon and nitrogen metabolism in rice (Oryza sativa L.)
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OmGOGAT-disruption in the ericoid mycorrhizal fungus Oidiodendron maius induces reorganization of the N pathway and reduces tolerance to heavy-metals
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71
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Oidiodendron maius
brenda
Yamaya, T.; Kusano, M.
Evidence supporting distinct functions of three cytosolic glutamine synthetases and two NADH-glutamate synthases in rice
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65
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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
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152
138-151
2014
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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9
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Arabidopsis thaliana
brenda
Garcia-Gutierrez, A.; Canovas, F.M.; Avila, C.
Glutamate synthases from conifers gene structure and phylogenetic studies
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19
65
2018
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Imagawa, F.; Minagawa, H.; Nakayama, Y.; Kanno, K.; Hayakawa, T.; Kojima, S.
Tos17 insertion in NADH-dependent glutamate synthase genes leads to an increase in grain protein content in rice
J. Cereal Sci.
84
38-43
2018
Oryza sativa Japonica Group (Q0DG35), Oryza sativa Japonica Group (Q0JKD0)
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brenda
Jiao, Y.; Chen, Y.; Ma, C.; Qin, J.; Nguyen, T.H.N.; Liu, D.; Gan, H.; Ding, S.; Luo, Z.B.
Phenylalanine as a nitrogen source induces root growth and nitrogen-use efficiency in Populus x canescens
Tree Physiol.
38
66-82
2018
Populus tremula x Populus alba (A1Y9J3)
brenda