1.4.1.2: glutamate dehydrogenase
This is an abbreviated version!
For detailed information about glutamate dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.2
-
1.4.1.2
-
ammonia
-
aminotransferase
-
giardia
-
deamination
-
dehydrogenases
-
malate
-
alpha-ketoglutarate
-
clostridium
-
difficile
-
assemblage
-
transaminase
-
succinate
-
duodenalis
-
adp
-
2-oxoglutarate
-
toxin
-
nitrate
-
stool
-
glutaminase
-
zoonotic
-
isocitrate
-
immunoassay
-
fecal
-
tpi
-
transamination
-
multilocus
-
toxigenic
-
neurospora
-
hyperinsulinism
-
triose
-
hypoglycemia
-
oxaloacetate
-
nadp-dependent
-
bilirubin
-
hexameric
-
hyperammonemia
-
giardiasis
-
triosephosphate
-
l-leucine
-
cryptosporidium
-
no3
-
aminooxyacetate
-
intestinalis
-
ribotype
-
quinoproteins
-
gamma-glutamyltransferase
-
glutaminolysis
-
diazoxide
-
degradation
-
agriculture
-
biotechnology
-
gaba-t
-
drug development
-
medicine
-
molecular biology
-
pancreatectomy
-
analysis
-
food industry
-
energy production
-
diagnostics
-
synthesis
- 1.4.1.2
- ammonia
- aminotransferase
- giardia
-
deamination
- dehydrogenases
- malate
- alpha-ketoglutarate
- clostridium
- difficile
-
assemblage
- transaminase
- succinate
- duodenalis
- adp
- 2-oxoglutarate
- toxin
- nitrate
-
stool
- glutaminase
-
zoonotic
- isocitrate
-
immunoassay
-
fecal
- tpi
-
transamination
-
multilocus
-
toxigenic
- neurospora
- hyperinsulinism
- triose
- hypoglycemia
- oxaloacetate
-
nadp-dependent
- bilirubin
-
hexameric
-
hyperammonemia
- giardiasis
-
triosephosphate
- l-leucine
- cryptosporidium
- no3
- aminooxyacetate
- intestinalis
-
ribotype
-
quinoproteins
- gamma-glutamyltransferase
-
glutaminolysis
- diazoxide
- degradation
- agriculture
- biotechnology
- gaba-t
- drug development
- medicine
- molecular biology
-
pancreatectomy
- analysis
- food industry
- energy production
- diagnostics
- synthesis
Reaction
Synonyms
At5g18170, AtGDH1, BpNADGDH, c, CCNA_00086, CsGDH, dehydrogenase, glutamate, GDH, GDH isoenzyme 1, GDH, NAD-dependent, gdh-1, gdh-2, GDH1, GDH2, Gdh2p, GDH3, GdhA, GDHB, GDHI, GdhZ, Glu dehydrogenase, GluD, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase (NAD), glutamate dehydrogenase 2, glutamate dehydrogenase alpha subunit, glutamate dehydrogenase beta subunit, glutamate dehydrogenase isoform 1, glutamate oxidoreductase, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2-nerve-specific GDH, house-keeping GDH, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, More, NAD(+)-dependent glutamate dehydrogenase, NAD(H)-dependent glutamate dehydrogenase, NAD+-dependant glutamate dehydrogenase, NAD+-dependent GDH, NAD+-dependent GDHX, NAD+-dependent GluDH, NAD+-dependent glutamate dehydrogenase, NAD+-GDH, NAD+-glutamate dehydrogenase, NAD+-specific GDH, NAD+-specific glutamate dehydrogenase, NAD-dependent GDH, NAD-dependent glutamate dehydrogenase, NAD-dependent glutamic dehydrogenase, NAD-dependent L-glutamate dehydrogenase, NAD-GDH, NAD-glutamate dehydrogenase, NAD-linked glutamate dehydrogenase, NAD-linked glutamic dehydrogenase, NAD-specific glutamate dehydrogenase, NAD-specific glutamic dehydrogenase, NAD-ylGdh2p, NAD:glutamate oxidoreductase, NADH-dependent GDH, NADH-dependent glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, NADH-linked glutamate dehydrogenase, OsGDH1, OsGDH2, OsGDH3, Pcal_1031, RocG, sco2999, Surface-associated protein PGAG1, t-GDH, type I GDH, YALI0E09603g, ylGDH2
ECTree
1.4.1.2 glutamate dehydrogenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.4.1.2 - glutamate dehydrogenase
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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
2-oxo-3-methylvalerate + NADPH + NH3
L-isoleucine + NADP+ + H2O
-
very low specificity of wild-type
-
-
?
2-oxo-iso-caproate + NADPH + NH3
L-norleucine + NADP+ + H2O
-
very low specificity of wild-type
-
-
?
2-oxo-iso-valerate + NADPH + NH3
L-leucine + NADP+ + H2O
-
low specificity of wild-type
-
-
?
2-oxocaproate + NH3 + NADH + H+
L-2-aminohexanoate + H2O + NAD+
1.3% of the activity with 2-oxoglutarate
-
-
r
2-oxovalerate + NH3 + NADH + H+
L-valine + H2O + NAD+
6.6% of the activity with 2-oxoglutarate
-
-
r
beta-phenylpyruvate + NADPH + NH3
L-phenylalanine + NADP+ + H2O
-
low specificity of wild-type
-
-
?
DL-norleucine + H2O + NAD+
? + NH3 + NADH + H+
-
1.6% activity compared to L-glutamate, pH 9.0
-
-
r
L-alanine + H2O + NAD+
? + NH3 + NADH + H+
-
0.27% activity compared to L-glutamate, pH 9.0
-
-
r
L-alpha-aminobutyrate + H2O + NAD+
? + NH3 + NADH + H+
-
2.3% activity compared to L-glutamate, pH 9.0
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
weak reaction
-
-
?
L-isoleucine + H2O + NAD+
2-oxo-3-methylvalerate + NH3 + NADH + H+
3.0% of the activity with L-glutamate
-
-
r
L-isoleucine + H2O + NAD+
? + NH3 + NADH + H+
-
0.95% activity compared to L-glutamate, pH 9.0
-
-
r
L-leucine + H2O + NAD+
2-oxo-iso-valerate + NH3 + NADH + H+
1.6% of the activity with L-glutamate
-
-
r
L-leucine + H2O + NAD+
2-oxoisovalerate + NH3 + NADH + H+
-
1.7% activity compared to L-glutamate, pH 9.0
-
-
r
L-methionine + H2O + NAD+
? + NH3 + NADH + H+
-
0.82% activity compared to L-glutamate, pH 9.0
-
-
r
L-norvaline + H2O + NAD+
? + NH3 + NADH + H+
-
17% activity compared to L-glutamate, pH 9.0
-
-
r
L-serine + H2O + NAD+
3-hydroxy-2-oxopropanoate + NH3 + NADH
-
deamination at 29% the rate of L-glutamate deamination
-
-
?
L-valine + H2O + NAD+
2-oxovalerate + NH3 + NADH + H+
31% of the activity with L-glutamate
-
-
r
L-valine + H2O + NAD+
? + NH3 + NADH + H+
-
1.6% activity compared to L-glutamate, pH 9.0
-
-
r
p-hydroxyphenylpyruvate + NADPH + NH3
L-tyrosine + NADP+ + H2O
-
very low specificity of wild-type
-
-
?
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
2.7% of the activity with 2-oxoglutarate
-
-
r
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
2.7% of the activity with 2-oxoglutarate
-
-
r
2-oxobutyrate + NADH + NH3
2-aminobutyrate + NAD+ + H2O
faint specificity
-
-
?
2-oxobutyrate + NADH + NH3
2-aminobutyrate + NAD+ + H2O
faint specificity
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
2fold increase in NADH-dependent GDH aminating activity 28 days after flowering
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
wild-type enzyme highly specific for 2-oxoglutarate
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
no significant activity of deamination reaction
-
-
ir
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
in conjugation with glutamine synthase, the glutamate dehydrogenase plays a major role in controlling the translocation of organic carbon and nitrogen metabolites in both vegetative and reproductive organs. It is possible that the presence of glutamate dehydrogenase in multivesicular bodies within the flower receptacle is important for the recycling of carbon and nitrogen molecules in senescing tissues in which the enzyme is generally induced
-
-
?
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
136% of the activtiy with L-glutamate
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
8.4% of the activity with L-glutamate
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
8.4% of the activity with L-glutamate
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?, r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
AtGDH1 activity in the forward reaction (oxidative deamination) is physiologically more relevant due to the high NAD+/NADH ratio in plant mitochondria
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
RocG is exclusively devoted to L-glutamate degradation rather than to its synthesis
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
control point for amino acid metabolism
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
glutamate oxidation is favoured
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
primary role in squid mantle muscle is in regulating the catabolism of amino acids for energy production
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
best substrate, pH 8.0
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
proposed mechanism involves hydrogen binding of each of the two carboxylic groups to tyrosyl residues. Histidine interacts with one of the N-hydrogens of the L-glutamate amino group
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
reaction cycle, overview
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
the enzyme may be linked to oxygen through an electron-transport system
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
Saccharolobus solfataricus MT-4 / DSM 5833
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
ir
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
strict substrate specificity
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
-
r
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
the amination reaction is preferred
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
r
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
ir
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
progressive decrease in NAD-GDH deaminating activity from flowering to maturity
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
deamination at 5% the rate of L-glutamate deamination
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
at 40% the rate
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
35% of the activity with L-glutamate
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
35% of the activity with L-glutamate
-
-
r
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
faint specificity
-
-
?
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
-
very low specificity of wild-type
-
-
?
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
faint specificity
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
faint specificity
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
-
very low specificity of wild-type
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
faint specificity
-
-
?
additional information
?
-
no activity with L-aspartate, L-alanine, L-valine and L-serine
-
-
?
additional information
?
-
-
no activity with L-aspartate, L-alanine, L-valine and L-serine
-
-
?
additional information
?
-
-
no specificity of wild-type for 2-ketohexonoate
-
-
?
additional information
?
-
-
RocG is able to bind to and concomitantly inactivate the activator protein GltC
-
-
?
additional information
?
-
no activity with L-aspartate, L-alanine, L-valine and L-serine
-
-
?
additional information
?
-
-
substrate specificity of partially purified enzyme, overview. The enzyme exhibits stereospecificity for the L-isomer. No activity with L-ornithine, L-lysine, L-proline, L-aspartic acid, L-alpha-aminoadipic acid, L-threonine, D-leucine, and DL-alpha-methylglutamic acid. The gamma-carboxyl group of glutamic acid facilitates the binding of this substrate to the enzyme through an electrostatic attraction between this negatively charged group and a positively charged group on the enzyme. Decrease or increase of the length of the carbon chain by a single methylene group (e.g., aspartic and alpha-aminoadipic acids) appears to abolish activity. The presence of a second positively charged group in the substrate, as in ornithine or lysine, interferes with binding to the enzyme
-
-
-
additional information
?
-
inert reaction with L-glutamine, L-aspartate, L-alanine, L-leucine, L-valine, L-lysine, L-2-aminobutyrate, L-methionine, L-ornithine, L-phenylalanine, L-arginine, L-tryptophan, L-methionine, L-histidine, D-glutamate, and D-aspartate, the enzyme is not active with NADP+
-
-
?
additional information
?
-
-
inert reaction with L-glutamine, L-aspartate, L-alanine, L-leucine, L-valine, L-lysine, L-2-aminobutyrate, L-methionine, L-ornithine, L-phenylalanine, L-arginine, L-tryptophan, L-methionine, L-histidine, D-glutamate, and D-aspartate, the enzyme is not active with NADP+
-
-
?
additional information
?
-
inert reaction with L-glutamine, L-aspartate, L-alanine, L-leucine, L-valine, L-lysine, L-2-aminobutyrate, L-methionine, L-ornithine, L-phenylalanine, L-arginine, L-tryptophan, L-methionine, L-histidine, D-glutamate, and D-aspartate, the enzyme is not active with NADP+
-
-
?
additional information
?
-
-
inert reaction with L-glutamine, L-aspartate, L-alanine, L-leucine, L-valine, L-lysine, L-2-aminobutyrate, L-methionine, L-ornithine, L-phenylalanine, L-arginine, L-tryptophan, L-methionine, L-histidine, D-glutamate, and D-aspartate, the enzyme is not active with NADP+
-
-
?
additional information
?
-
-
no or poor activity with NADP+/NADPH in both reaction directions. The enzyme also shows low activity with L-norvaline, L-2-aminobutyrate, L-valine, L-isoleucine, and L-leucine as substrates for oxidative deamination, and with 2-oxovalerate, 2-oxobutyrate, and 2-oxocaproate, for reducive amination, substrate specificity, overview. No activity with L-2-aminobutyrate, L-valine, L-isoleucine, L-leucine, L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate and pyruvate
-
-
?
additional information
?
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no or poor activity with NADP+/NADPH in both reaction directions. The enzyme also shows low activity with L-norvaline, L-2-aminobutyrate, L-valine, L-isoleucine, and L-leucine as substrates for oxidative deamination, and with 2-oxovalerate, 2-oxobutyrate, and 2-oxocaproate, for reducive amination, substrate specificity, overview. No activity with L-2-aminobutyrate, L-valine, L-isoleucine, L-leucine, L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate and pyruvate
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additional information
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in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
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additional information
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L-alpha-amino-gamma-nitroaminobutyrate deamination at 0.5% the rate of deamination of L-glutamate
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