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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-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
2-oxobutyrate + NADH + NH3
2-aminobutyrate + NAD+ + H2O
2-oxocaproate + NH3 + NADH + H+
L-2-aminohexanoate + H2O + NAD+
1.3% of the activity with 2-oxoglutarate
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
2-oxoglutarate + NH4+ + NADH
L-glutamate + NAD+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
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-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
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 + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
-
weak reaction
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
-
-
-
-
r
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+
2-oxopentanoate + NH3 + NADH
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
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
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
p-hydroxyphenylpyruvate + NADPH + NH3
L-tyrosine + NADP+ + H2O
-
very low specificity of wild-type
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
additional information
?
-
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
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
2fold increase in NADH-dependent GDH aminating activity 28 days after flowering
-
-
r
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
wild-type enzyme highly specific for 2-oxoglutarate
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
no significant activity of deamination reaction
-
-
ir
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
-
-
-
-
?
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
L-glutamate + H2O + NAD+
-
-
-
r
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+
-
-
-
-
?
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
?
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
-
-
-
-
?
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(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
-
-
-
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
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
-
-
-
-
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+
-
-
-
-
?
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+
Apodachlya sp.
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
-
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+
-
-
-
-
?
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+
-
-
-
-
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+
-
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+
-
-
-
-
r
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+
-
-
-
?
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+
-
-
-
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+
-
-
-
-
?
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+
-
-
-
?
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+
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+
-
-
-
-
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+
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
-
?
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+
-
the enzyme may be linked to oxygen through an electron-transport system
-
-
?
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+
-
-
-
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+
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
-
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+
-
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
-
strict substrate specificity
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
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
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
-
-
-
-
r
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
ir
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
ir
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
?
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
progressive decrease in NAD-GDH deaminating activity from flowering to maturity
-
-
r
L-glutamate + NAD+ + H2O
2-oxoglutarate + NADH + NH3
-
-
-
-
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
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
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
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
-
L-alpha-amino-gamma-nitroaminobutyrate deamination at 0.5% the rate of deamination of L-glutamate
-
-
?
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2-methyl-2,4-pentanediol
8.5 mM, 94% residual activity. the sequence contains several binding sites for 2-methyl-2,4-pentanediol
2-Methyleneglutarate
-
potent competitive inhibitor
3,3'-[(2-bromobenzene-1,4-diyl)di(E)ethene-2,1-diyl]bis(6-hydroxybenzoic acid)
-
i.e. BSB
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
5,5'-dithiobis(2-nitrobenzoate)
alpha,gamma-Diethyl glutamate
-
-
ATP/GTP-competitive inhibitor of casein kinase-2
-
-
-
aurintricarboxylic acid
-
-
D-asparagine
93% activity in the presence of 10 mM D-asparagine
D-Aspartate
90% activity in the presence of 10 mM D-aspartate
D-glutamine
95% activity in the presence of 10 mM D-glutamine
diethyl dicarbonate
-
inactivation follows pseudo-first-order kinetics
DTNB
inactivation via blocking of the only two Cys residues, Cys144 in helix alpha7a of domain I, the substrate-binding domain, and Cys320 in a loop that connects betak and alpha13 in domain II, the coenzyme-binding domain
epicatechin-3-monogallate
-
-
epicatechin-monogallate
-
-
epigallocatechin-3,5-digallate
-
-
epigallocatechin-3-gallate
-
-
ethaverine hydrochloride
-
-
ethyl acetimidate
-
inactivation with ethyl acetimidate shows pseudo-first-order kinetics
glutathione
-
reduces increase in GDH activity due to Hg
glycogen accumulation regulator
GarA, native or unphosphorylated GarA is able to interact with NAD+-GDH causing a reduction in NAD+-GDH activity by altering the affinity of the enzyme for its substrate. This binding is prevented by the phosphorylation of GarA by PknG
-
guanidine hydrochloride
-
72°C, almost complete loss of activity by addition of more than 3 M
KCl
-
3 M, 75% inhibition
L-glutamate
substrate inhibition at L-glutamate concentrations above 20 mM
L-glutamine
89% activity in the presence of 10 mM L-glutamine
L-ornithine
83% activity in the presence of 10 mM L-ornithine
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
TLCK
NaCl
-
3 M, 89% inhibition
NADP+
-
non-competitive versus L-glutamate, non-competitive versus NAD+
NADPH
the wrong cofactor, NADPH, without the correct binding pocket to receive its 2'-phosphate, finds an alternative and catalytically unproductive way of occupying the coenzyme site
p-Aminomercuribenzoate
-
-
p-chloromercuribenzoate
-
-
phosphoenolpyruvate
-
weak
Tetranitromethane
-
rapid loss of enzymatic activity versus time at various concentrations of modifier, showing pseudo-first-order kinetics
2-oxoglutarate
-
non-competitive versus L-glutamate, competitive versus NAD+
2-oxoglutarate
substrate inhibition
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
ADP
-
-
Al3+
-
as increasing the Al3+ concentration, the activity of GDH is firstly inhibited (at less than 0.03 mM), then activated (0.03-0.08 mM), and finally inhibited (above 0.08 mM) in the Tris-HCl buffer solution at pH 6.5 and 7.5
Al3+
-
inhibits the enzyme activity in the absence of Hg
AMP
-
-
ATP
-
weak
bithionol
-
-
bithionol
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
bithionol
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
bithionol
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one or bithionol, respectively, bind as pairs of stacked compounds at hexameric 2-fold axes between the dimers of subunits
Ca2+
0.1 mM, 82% residual activity; 8% inhibition at 0.1 mM, 23% at 1 mM
Ca2+
-
activation of reductive amination; slight inhibition of oxidative deamination
Ca2+
-
activation of reductive amination; no effect on oxidative deamination
citrate
67% activity in the presence of 10 mM citrate
citrate
-
inhibition of amination, no effect on deamination
Co2+
0.1 mM, 77% residual activity; 23% inhibition at 0.1 mM
Co2+
82% activity in the presence of 1 mM Co2+
Cu2+
0.1 mM, 65% residual activity; 35% inhibition at 0.1 mM
D-glutamate
-
non-competitive versus L-glutamate, non-competitive versus NAD+
D-glutamate
94% activity in the presence of 10 mM D-glutamate
EDTA
-
-
fumarate
-
amination
fumarate
-
non-competitive versus L-glutamate, competitive versus NAD+
fumarate
32% activity in the presence of 10 mM fumarate
glutamate
-
-
glutamine
-
amination
glutamine
-
reduces increase in GDH activity due to Hg
Glutarate
-
uncompetitive versus L-glutamate, competitive versus NAD+
Glutarate
-
competitive inhibitor
GTP
-
-
Hexachlorophene
-
-
Hexachlorophene
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves
Hexachlorophene
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves
Hexachlorophene
-
inhibits GDH in a non-competitive manner with the Vmax being greatly affected without a very large change in Km. Crystal structures discloses that hexachlorophene forms a ring around the internal cavity in GDH through aromatic stacking interactions between the drug and GDH as well as between the drug molecules themselves
Hg2+
-
-
Hg2+
no activity in the presence of 1 mM Hg2+
Hg2+
1 mM, complete loss of activtiy for wild-type. 8fold increase in activity for mutant C1141T
isocitrate
-
-
isocitrate
49% activity in the presence of 10 mM isocitrate
isophthalate
-
-
isophthalate
-
potent in vitro inhibitor
L-aspartate
-
weak
malate
-
non-competitive versus L-glutamate, non-competitive versus NAD+
malate
65% activity in the presence of 10 mM malate
malate
10 mM, 75% residual activity
Mg2+
-
-
Mg2+
64% activity in the presence of 1 mM Mg2+
Mn2+
52% activity in the presence of 1 mM Mn2+
N-ethylmaleimide
-
-
NAD+
-
-
NADH
-
-
NH4+
-
-
Ni2+
77% activity in the presence of 1 mM Ni2+
oxaloacetate
-
amination
oxaloacetate
-
non-competitive versus L-glutamate, non-competitive versus NAD+
oxaloacetate
10 mM, 60% residual activity
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
Pyruvic acid
-
-
succinate
-
non-competitive versus L-glutamate, non-competitive versus NAD+
succinate
36% activity in the presence of 10 mM succinate
Zn2+
-
-
Zn2+
0.1 mM, 51% residual activity; 49% inhibition at 0.1 mM
additional information
not inhibitory: Mn2+
-
additional information
-
not inhibitory: Mn2+
-
additional information
-
no inhibition or activation in the presence of 500 mM AMP, ADP, ATP, cyclic-AMP, GMP, GDP or GTP
-
additional information
-
GTP, ATP, ADP and AMP do not affect the activity
-
additional information
not inhibited by NAD+
-
additional information
-
not inhibited by NAD+
-
additional information
-
Met sulfoximine and azaserine do not affect the aminating and deaminating activities of GDH
-
additional information
-
strong inhibition by increasing ionic strength
-
additional information
-
increase in GDH activity due to Hg remains unaffected by the supply of sucrose
-
additional information
-
no inhibition by GTP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Al3+
-
GDH is activated at 0.03-0.08 mM in the Tris-HCl buffer solution at pH 6.5 and 7.5
ATP
-
activates in presence of 3 M NaCl or 3 M Kcl, slight activation in absence of salts
D-arginine
212% activity in the presence of 10 mM D-arginine
glycerol
activates at 10%
guanidine hydrochloride
-
activates
H2O2
-
increase in the aminating GDH activity correlating with gene expression, in a dose-dependent manner
heating
-
at 90°C the activity of the recombinant enzyme increases to a level comparable to that of the native enzyme
-
isocitrate
10 M, 112% of initial activity
L-His
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
L-Leu
-
activates in presence of 3 M NaCl, 3 M Kcl or in absence of salts
NaCl
-
high NaCl induces the formation of reactive oxygen species, which in turn induces the synthesis of the alpha-subunit of GDH
NaNO3
GDH1 transcripts slightly and slowly increase by 2fold after N nutrition addition while GDH2 mRNA is not affected
NH3
-
GDH is activated by excess ammonia
NH4Cl
rapid and marked increase in the accumulation of mRNAs for GDH1 and GDH2 after supply
NH4NO3
-
increases the NADH-GDH activity in the presence of Hg
tetrahydrofuran
-
activates
Zn2+
224% activity in the presence of 1 mM Zn2+
ADP
-
-
ADP
-
ADP can reverse inhibition
ADP
-
absolute requirement as cofactor
ADP
-
absolute requirement as cofactor
ADP
-
activates in presence of 3 M NaCl or 3 M KCl. Inhibition in absence of salts
alkalized extract
-
from the tuber of Corydalis ternata, activates the hGDH1 up to 3.2fold and hGDH2 up to 4.1fold, hGDH2 is more sensitively affected by 1 mM ADP than hGDH1 on the activation by alkalized extracts
-
alkalized extract
-
from the tuber of Corydalis ternata, increases GDH activity 2.4fold after one year of feeding
-
AMP
-
stimulation
ethylene
-
induces protein expression
ethylene
-
increase in the expression of GDH and the aminating GDH activity
jasmonic acid
-
-
jasmonic acid
-
5 mM, induces protein expression
jasmonic acid
-
increase in the expression of GDH and the aminating GDH activity
L-arginine
-
-
L-arginine
936% activity in the presence of 10 mM L-arginine
L-asparagine
-
-
L-asparagine
118% activity in the presence of 10 mM L-asparagine
L-aspartate
1735% activity in the presence of 10 mM L-aspartate
L-aspartate
catalytic activator, 2fold activation at 0.1 mM, effect on enzyme kinetics, overview
L-cysteine
-
stimulates deamination
L-histidine
-
-
L-histidine
155% activity in the presence of 10 mM L-histidine
L-lysine
-
-
L-lysine
161% activity in the presence of 10 mM L-lysine
L-methionine
-
-
L-methionine
206% activity in the presence of 10 mM L-methionine
L-tryptophan
-
-
L-tryptophan
235% activity in the presence of 10 mM L-tryptophan
NH4+
-
the activity of glutamate dehydrogenase (GDH) in the ammonium-tolerant species Myriophyllum spicatum leaves performs a dose-response curve with increase of 169% for NADH-dependent GDH with the [NH4+-N] increasing from 0 to 100 mg/l, while glutamine synthetase (GS) activity slightly changes. Compared to that, for the ammonium-sensitive species, Potamogeton lucens, the activity of GDH records no major changes, while the GS increases slightly (17%)
NH4+
-
the activity of glutamate dehydrogenase (GDH) in the ammonium-tolerant species Myriophyllum spicatum leaves performs a dose-response curve with increase of 169% for NADH-dependent GDH with the [NH4+-N] increasing from 0 to 100 mg/l, while glutamine synthetase (GS) activity slightly changes. Compared to that, for the ammonium-sensitive species, Potamogeton lucens, the activity of GDH records no major changes, while the GS increases slightly (17%)
protopine
-
activates the human GDH isozymes, but to a less extent
protopine
-
increases GDH activity 1.6fold
salicylic acid
-
-
salicylic acid
-
induces protein expression
salicylic acid
-
increase in the expression of GDH
Urea
-
at 5 M the activity of the recombinant enzyme increases to a level comparable to that of the native enzyme, urea-induced activation of recombinant GDH is irreversible
Urea
-
activates the enzyme irreversibly at 5 M
Urea
-
72°C, maximal enhancement at 2 mM
additional information
-
no inhibition or activation in the presence of 500 mM AMP, ADP, ATP, cyclic-AMP, GMP, GDP or GTP
-
additional information
-
cryptogein and Onozuka R10 induce GDH expression, GDH activity is correlated with GDH expression and the GDH enzyme preferentially catalyses the aminating reaction
-
additional information
-
GDH mRNA accumulates preferentially in plants inoculated with the avirulent Pseudomonas syringae pv. syringae CFBP3077 (hrp+) and the virulent Pseudomonas syringae pv. tabaci CFBP1503 strains, induction of GDH expression by bacterial infection dependeds on the hrp- genotype, but not on the virulence/avirulence genotype
-
additional information
-
leaf GDH aminating-activity increases, whereas deaminating-activity is not affected by infection with viruses CMV, TEV, and PVY
-
additional information
prolonged dark-stress increases GDH activity, more likely due to resistance of the GDH protein to stress-induced proteolysis, rather than to post-translational up-regulation
-
additional information
prolonged dark-stress increases GDH activity, more likely due to resistance of the GDH protein to stress-induced proteolysis, rather than to post-translational up-regulation
-
additional information
-
prolonged dark-stress increases GDH activity, more likely due to resistance of the GDH protein to stress-induced proteolysis, rather than to post-translational up-regulation
-
additional information
-
the enzyme is activated by heat above 70°C, urea and organic solvents, but not by salts. Activation of recombinant enzyme by urea and heat, that is purified as inactive enzyme at 4°C
-
additional information
-
no activation by ADP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0008 - 606
2-oxoglutarate
0.000011 - 1349
L-glutamate
additional information
additional information
-
0.0008
2-oxoglutarate
pH 8.5, 40°C, recombinant enzyme in presence of DMSO
0.00111
2-oxoglutarate
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.00131
2-oxoglutarate
-
animals treated with protopine
0.00138
2-oxoglutarate
-
control group
0.0034
2-oxoglutarate
pH 8.5, 40°C, recombinant enzyme
0.041
2-oxoglutarate
pH 6.5, 25°C, recombinant enzyme, in presence of 10 mM L-aspartate
0.0862
2-oxoglutarate
-
mutant D165N
0.103
2-oxoglutarate
-
pH 7, 25°C
0.125
2-oxoglutarate
-
wild-type
0.65
2-oxoglutarate
-
wild-type
0.65
2-oxoglutarate
wild-type
0.75
2-oxoglutarate
-
activated NAD-GDH
0.92
2-oxoglutarate
-
pH 9.5, 50°C, recombinant enzyme
0.92
2-oxoglutarate
pH 9.5, 50°C
0.93
2-oxoglutarate
mutant E27F
1.22
2-oxoglutarate
mutant Q144R
1.9
2-oxoglutarate
-
non-activated NAD-GDH
2.36
2-oxoglutarate
-
NAD+-dependent enzyme
2.36
2-oxoglutarate
-
pH 8.0, 20°C
2.85
2-oxoglutarate
-
wild-type CsGDH, Vmax: 546 micromol/min/mg, pH 8.0, 25°C
3.12
2-oxoglutarate
-
pH 8.0, 23°C
5.6
2-oxoglutarate
-
pH 8.0
100
2-oxoglutarate
-
mutant M101S
285
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25°C
606
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25°C
5.82
glutamate
-
pH 7, 25°C
0.000011
L-glutamate
pH 9.0, 40°C, recombinant enzyme
0.000025
L-glutamate
pH 9.0, 40°C, recombinant enzyme in presence of DMSO
0.00299
L-glutamate
-
animals treated with protopine
0.00302
L-glutamate
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.00321
L-glutamate
-
control group
0.16
L-glutamate
-
native enzyme
0.16
L-glutamate
-
recombinant, heat-activated enzyme
0.18
L-glutamate
-
recombinant, urea-activated enzyme
0.34
L-glutamate
wild-type
0.39
L-glutamate
0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5
1.06
L-glutamate
0.005 mM inhibitor biothionol, Vmax: 0.1, pH 7.5
1.17
L-glutamate
0.003 mM inhibitor biothionol, Vmax: 0.14, pH 7.5
1.27
L-glutamate
0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.05, pH 7.5
1.38
L-glutamate
0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5
1.38
L-glutamate
without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.17, pH 7.5
1.39
L-glutamate
-
wild-type CsGDH, Vmax: 47.1 micromol/min/mg, pH 8.0, 25°C
1.53
L-glutamate
0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5
1.62
L-glutamate
without inhibitor biothionol, Vmax: 0.18, pH 7.5
2.5 - 5
L-glutamate
pH 7.5, 25°C
2.5 - 5
L-glutamate
with NAD+, recombinant enzyme, pH and temperature not specified in the publication
2.66
L-glutamate
-
mutant D165N
3.25
L-glutamate
-
mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.25
L-glutamate
-
wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.3
L-glutamate
-
mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.41
L-glutamate
-
mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.7 - 5
L-glutamate
-
mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
3.97
L-glutamate
-
wild-type
5.1
L-glutamate
mutant C872R, pH 9.0, 25°C
5.2
L-glutamate
mutant C1141T, pH 9.0, 25°C
5.3
L-glutamate
-
pH 10.5, 50°C, recombinant enzyme
5.3
L-glutamate
pH 10.5, 50°C
5.4
L-glutamate
mutant C825G, pH 9.0, 25°C
6.1
L-glutamate
wild-type, pH 9.0, 25°C
6.8
L-glutamate
mutant D869A, pH 9.0, 25°C
7.1
L-glutamate
in the presence of 5 mM NAD+, in 100 mM glycine/NaOH (pH 9.5), at 25°C
7.2
L-glutamate
mutant V1139A, pH 9.0, 25°C
18.2
L-glutamate
-
mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
28.6
L-glutamate
-
NAD+-dependent enzyme
28.6
L-glutamate
-
pH 8.0, 20°C
33.33
L-glutamate
-
pH 8.0, 23°C
1349
L-glutamate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C
0.018
NAD+
-
recombinant, urea-activated enzyme
0.019
NAD+
-
native enzyme
0.021
NAD+
-
recombinant, heat-activated enzyme
0.028
NAD+
-
pH 10.5, 50°C, recombinant enzyme
0.076
NAD+
-
mutant D165N
0.112
NAD+
pH 9.0, 40°C, recombinant enzyme in presence of DMSO
0.118
NAD+
pH 9.0, 40°C, recombinant enzyme
0.125
NAD+
-
wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.138
NAD+
-
mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.14
NAD+
0.008 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.04, pH 7.5
0.168
NAD+
-
wild-type CsGDH, Vmax: 40.6 micromol/min/mg, pH 8.0, 25°C
0.22
NAD+
-
mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.23
NAD+
-
mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.23
NAD+
0.0015 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.13, pH 7.5
0.26
NAD+
0.004 mM inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.09, pH 7.5
0.26
NAD+
0.009 mM inhibitor biothionol, Vmax: 0.05, pH 7.5
0.31
NAD+
without inhibitor 3-(3,5-dibromo)-4-hydroxybenzylidine-5-iodo-1,3-dihydro-indol-2-one, Vmax: 0.24, pH 7.5
0.31
NAD+
without inhibitor biothionol, Vmax: 0.24, pH 7.5
0.35
NAD+
-
mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.36
NAD+
0.005 mM inhibitor biothionol, Vmax: 0.13, pH 7.5
0.4
NAD+
-
mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C
0.43
NAD+
0.003 mM inhibitor biothionol, Vmax: 0.22, pH 7.5
0.5
NAD+
-
NAD+-dependent enzyme
1.2
NAD+
mutant C825G, pH 9.0, 25°C
1.2
NAD+
mutant V1139A, pH 9.0, 25°C
1.3
NAD+
wild-type, pH 9.0, 25°C
1.3
NAD+
mutant C872R, pH 9.0, 25°C
1.5
NAD+
mutant D869A, pH 9.0, 25°C
2.1
NAD+
in the presence of 20 mM L-glutamate, in 100 mM glycine/NaOH (pH 9.5), at 25°C
2.1
NAD+
mutant C1141T, pH 9.0, 25°C
0.001
NADH
-
pH 9.5, 50°C, recombinant enzyme
0.0044
NADH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.0056
NADH
-
mutant D165N
0.0076
NADH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.009
NADH
pH 8.5, 40°C, recombinant enzyme in presence of DMSO
0.0123
NADH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.014
NADH
pH 8.5, 40°C, recombinant enzyme
0.018
NADH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.018
NADH
-
pH 6.0, 25°C, mutant P262S
0.02
NADH
-
pH 7.0, 25°C, recombinant wild-type enzyme
0.022
NADH
-
pH 6.0, 25°C, mutant D263K
0.023
NADH
-
pH 7.0, 25°C, mutant D263K
0.025
NADH
-
pH 7.0, 25°C, mutant A242G
0.028
NADH
-
pH 6.0, 25°C, mutant F238S
0.034
NADH
-
pH 6.0, 25°C, mutant A242G
0.035
NADH
-
pH 7.0, 25°C, mutant F238S/P262S
0.036
NADH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.036
NADH
-
pH 6.0, 25°C, recombinant wild-type enzyme
0.03609
NADH
-
control group
0.037
NADH
-
non-activated NAD-GDH
0.03785
NADH
-
animals treated with protopine
0.03833
NADH
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.0385
NADH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.04
NADH
-
pH 7.0, 25°C, mutant F238S
0.047
NADH
-
pH 7.0, 25°C, mutant P262S
0.048
NADH
-
pH 6.0, 25°C, mutant F238S/P262S
0.055
NADH
-
wild-type CsGDH, Vmax: 285 micromol/min/mg, pH 8.0, 25°C
0.078
NADH
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.085
NADH
-
pH 8.0, 25°C, mutant A242G
0.09
NADH
-
activated NAD-GDH
0.091
NADH
-
mutant M101S
0.091
NADH
-
pH 8.0, 25°C, mutant D263K
0.142
NADH
-
pH 8.0, 25°C, mutant P262S
0.204
NADH
-
pH 8.0, 25°C, mutant F238S/P262S
0.23
NADH
-
pH 8.0, 25°C, mutant F238S
0.163
NADP+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C
0.0384
NADPH
-
mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.053
NADPH
-
mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.238
NADPH
-
mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.431
NADPH
-
mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.476
NADPH
-
mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.51
NADPH
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25°C
1.64
NADPH
-
wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride
0.00013
NH3
pH 8.5, 40°C, recombinant enzyme in presence of DMSO
0.00035
NH3
pH 8.5, 40°C, recombinant enzyme
9.8
NH3
-
pH 9.5, 50°C, recombinant enzyme
33.9
NH3
as NH4+, pH 6.5, 25°C, recombinant enzyme, in absence of L-aspartate
0.00528
NH4+
-
animals treated with alkalized extract from the tuber of Corydalis ternata
0.0054
NH4+
-
animals treated with protopine
0.00613
NH4+
-
control group
0.033
NH4+
-
for 200 mM NH4+
12.9
NH4+
-
wild-type CsGDH, Vmax: 307 micromol/min/mg, pH 8.0, 25°C
22.8
NH4+
-
non-activated NAD-GDH
24.6
NH4+
-
NAD+-dependent enzyme
25.6
NH4+
-
activated NAD-GDH
96
NH4+
-
from double-reciprocal plots for concentrations between 5 mM and 200 mM
304
NH4+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25°C
2.27
oxaloacetate
-
mutant M101S
4.16
oxaloacetate
-
mutant G82K
additional information
additional information
-
no significant changes in Km values between groups treated with alkalized extract from the tuber of Corydalis ternata or protopine and control groups
-
additional information
additional information
-
wild-type Vmax: 23.71 (pH 7), 35.16 (pH 9)
-
additional information
additional information
dissociation constants of wild-type and mutant enzymes for different coenzymes, overview
-
additional information
additional information
the enzyme shows positive cooperativity towards 2-oxoglutarate and NADH, and Michaelis-Menten type kinetics with ammonium chloride in the absence of catalytic activator L-aspartate. L-aspartate effect on enzyme kinetics, overview
-
additional information
additional information
-
the enzyme shows positive cooperativity towards 2-oxoglutarate and NADH, and Michaelis-Menten type kinetics with ammonium chloride in the absence of catalytic activator L-aspartate. L-aspartate effect on enzyme kinetics, overview
-
additional information
additional information
-
cofactor kinetics, overview
-
additional information
additional information
-
cofactor kinetics, overview
-
additional information
additional information
-
cofactor kinetics, overview. Even without the heterotropic antenna responsible for allosteric regulation in mammalian enzymes, the GDH is emphatically still allosteric. The Eadie-Hofstee plot for NAD+ is strongly non-linear.Att pH 9.0 there is almost total positive co-operativity with glutamate, with a Hill coefficient close to the theoretical maximum of 6 for a hexamer
-
additional information
additional information
-
enzyme kinetics of wild-tyype and mutant enzymes with NADPH, overview
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes with NADH/NAD+ and NADPH/NADP+, overview
-
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0.0003
-
mutant D165N overexpressed at 8°C
0.012
-
2-oxoglutarate, mutant M101K
0.014
-
2-oxoglutarate, mutant K80R
0.019
-
2-oxoglutarate, mutant G82R and M101S
0.026
-
2-oxoglutarate, mutant G82K
0.034
-
mutant D165N overexpressed at 37°C
0.047
-
mutant D165N overexpressed at 23°C
0.0495 - 0.133
-
pH 8.2, 30°C
0.077
NADP-linked GDH activity
0.21
-
on L-aspartate, mutant M101S
0.29
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.32
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.34
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.39
-
on L-aspartate, mutant G82K
0.49
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NAD+
0.5
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
0.51
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
0.62
recombinant enzyme from crude cell extract, at 25°C
0.73
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
0.77
NAD-linked GDH activity
0.84
-
with alkalized extract from the tuber of Corydalis ternata
0.87
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.9
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
0.97
in the presence of antibiotics and ammonia
1.12
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.14
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.23
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
1.32
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
1.53
-
mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
1.83
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
101.8
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
102
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
11
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
119.5
-
in the presence of 0.1 mM Hg
12
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
12.5
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
15
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
155
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
17.6
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
170.6
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutamine
171.4
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in the presence of 0.1 mM Hg and in the presence of 0.1 mM AlCl3
174
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
19
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mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
19.7
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in the absence of Hg and in the presence of 0.1 mM AlCl3
2.16
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mutant enzyme D245K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.26
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mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.3
-
mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
2.98
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20
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mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
20.1
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
20.6
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
243.4
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in the presence of 0.1 mM Hg and in the presence of NH4NO3
25
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in the presence of 0.001 mM Hg and in the presence of NH4NO3
25.3
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mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
26.7
-
in the presence of 0.001 mM Hg
3
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mutant enzyme E243R, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.05
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
3.1
purified recombinant enzyme, at 25°C
3.27
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
3.41
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
3.54
-
recombinant, urea-activated enzyme
3.65
-
recombinant, heat-activated enzyme
3.82
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
30
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
328.2
-
in the presence of 0.1 mM Hg and in the presence of 5 mM sucrose
34
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
34.2
-
in the absence of Hg
35
recombinant enzyme purified from Haloferax volcanii, pH 8.5, 40°C
4.1
-
mutant enzyme E243R, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
4.93
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
440
-
2-oxoglutarate, wild-type
5
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
5.2
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
5.8
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
50
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
52.9
-
in the absence of Hg and in the presence of 5 mM sucrose
54.6
-
in the presence of 0.01 mM Hg
56
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
56.5
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
58
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NADP+
58.6
-
in the absence of Hg and in the presence of 5 mM glutathione
59.4
-
in the absence of Hg and in the presence of 5 mM glutamine
6.52
recombinant enzyme in Haloferax volcanii, pH 8.5, 40°C
6.78
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
62
-
mutant enzyme W244S, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
65.8
-
in the absence of Hg and in the presence of NH4NO3
68
-
mutant enzyme D245K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
7.2
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
70.94
-
in the presence of 0.1 mM Hg and in the presence of 5 mM glutathione
72
-
in the presence of 0.01 mM Hg and in the presence of NH4NO3
89.3
purified recombinant enzyme
9.01
-
mutant enzyme E243K, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.6
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.5
9.8
-
wild type enzyme, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 6.0
90
-
mutant enzyme E243D, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
0.33
-
mutant enzyme W244S, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.0
0.33
-
wild type enzyme, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
1.47
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 7.5
1.47
-
mutant enzyme E243D, with 0.1 mM NADPH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
104
-
GDH II
104
purified native enzyme
248
-
-
248
-
NAD+-dependent enzyme
54
-
GDH-II
54
-
mutant enzyme E243K, with 0.1 mM NADH, 20 mM oxoglutarate and 100 mM ammonium chloride at pH 8.0
additional information
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additional information
Apodachlya sp.
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additional information
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additional information
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additional information
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glucose withdrawal stimulates GDH activity
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additional information
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additional information
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GDH activity is markedly increased in Pseudomonas fluorescens cultures exposed to menadione-containing media containing Arg, Glu and Pro. When NH4+ is utilized as the nitrogen source, both alpha-ketoglutarate dehydrogenase and GDH levels are diminished. These enzymatic profiles are reversed when control cells are incubated in menadione media
additional information
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additional information
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additional information
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additional information
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additional information
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evolution
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NAD+-dependent, NADP+-dependent and dual-specificity GDHs, EC 1.4.1.2-1.4.1.4 are closely related and a few site-directed mutations can reverse specificity, overview. Specificity for NAD+ or for NADP+ has probably emerged repeatedly during evolution, using different structural solutions on different occasions. an acidic P7 residue usually hydrogen bonds to the 2'- and 3'-hydroxyls, may permit binding of NAD+ only, NADP+ only, or in higher animals both
evolution
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NAD+-dependent, NADP+-dependent and dual-specificity GDHs, EC 1.4.1.2-1.4.1.4 are closely related and a few site-directed mutations can reverse specificity, overview. Specificity for NAD+ or for NADP+ has probably emerged repeatedly during evolution, using different structural solutions on different occasions. an acidic P7 residue usually hydrogen bonds to the 2'- and 3'-hydroxyls, may permit binding of NAD+ only, NADP+ only, or in higher animals both
evolution
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the enzyme belongs to the family of amino acid dehydrogenases
evolution
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the enzyme belongs to the family of amino acid dehydrogenases
evolution
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the enzyme belongs to the family of amino acid dehydrogenases
evolution
BpNADGDH gives over 65% identity scores with fungal NAD-dependent GDHs
evolution
GDHs are members of a superfamily of ELFV (Glu/Leu/Phe/Val) amino acid dehydrogenases and are subdivided into three subclasses, based on coenzyme specificity: NAD+-specific, NAD+/NADP+ dual-specific, and NADP+-specific. The mitochondrial AtGDH1 isozyme from Arabidopsis thaliana is NAD+-specific. Arabidopsis thaliana expresses three GDH isozymes (AtGDH1-3) targeted to mitochondria, of which AtGDH2 has an extra EF-hand motif and is stimulated by calcium, while AtGDH1's sensitivity to calcium is negligible. In vivo the AtGDH1-3 enzymes form homo- and heterohexamers of varied composition. Phylogenetic analysis of GDHs in plants. Plants have distinct isozymes of GDH that are either NAD or NADP-specific. NAD-specific GDHs are localized in mitochondria, whereas NADP-specific GDHs exist in chloroplasts. The sequence region 257-264 in AtGDH1 and AtGDH2, which directly precedes the EF-hand motif in AtGDH2 (residues 265-277), is the most altered region of AtGDH2 in comparison with AtGDH1
evolution
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in 39 wild isolates of Lactococcus lactis from raw milk cheeses, only 25% of the isolates are glutamate dehydrogenase positive with NAD+ as the preferred cofactor. Lactococcus lactis IFPL953 shows the highest NAD-GDH activity
evolution
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in 39 wild isolates of Lactococcus lactis from raw milk cheeses, only 25% of the isolates are glutamate dehydrogenase positive with NAD+ as the preferred cofactor. Lactococcus lactis IFPL953 shows the highest NAD-GDH activity
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malfunction
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a gdh1-2-3 triple mutant exhibits major differences to the wild-type in gene transcription and metabolite concentrations, and these differences appear to originate in the roots, metabolic profile of the gdh1-2-3 triple mutant, overview
malfunction
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when one or two of the three root isoenzymes are missing from the mutants, the remaining isoenzymes compensate for this deficiency
malfunction
the disruption of GDH2 was not deleterious to glutamate homeostasis. Mutant gdh2DELTA cells present wild-type growth and do not display any deficiencies due to glutamate homeostasis impairment neither under glucose nor under non-fermentable carbon sources. Deletion of GDH2 gene in a gdh3DELTA background increases the resistance under thermal or oxidative stress by decreasing ROS accumulation. The apoptosis is suppressed by GDH2 deletion through the elevated levels of glutamate and glutathione present in the double mutant. Under the tested conditions, deletion of GDH2 compensates the depletion of intracellular glutamate and glutathione (GSH) followed by stress-induced apoptotic cell death reinforcing further the idea that Gdh2p is responsible only for glutamate catabolism and not its production
malfunction
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the disruption of GDH2 was not deleterious to glutamate homeostasis. Mutant gdh2DELTA cells present wild-type growth and do not display any deficiencies due to glutamate homeostasis impairment neither under glucose nor under non-fermentable carbon sources. Deletion of GDH2 gene in a gdh3DELTA background increases the resistance under thermal or oxidative stress by decreasing ROS accumulation. The apoptosis is suppressed by GDH2 deletion through the elevated levels of glutamate and glutathione present in the double mutant. Under the tested conditions, deletion of GDH2 compensates the depletion of intracellular glutamate and glutathione (GSH) followed by stress-induced apoptotic cell death reinforcing further the idea that Gdh2p is responsible only for glutamate catabolism and not its production
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metabolism
NAD+-GDH plays an important role in nitrogen assimilation rather than glutamate catabolism, and is involved in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH. The specific activity of the deaminating NAD+-GDH reaction is mostly independent of nitrogen availability, overview, overview
metabolism
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together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP
metabolism
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together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP
metabolism
GDH contributes to Glu homeostasis and plays a significant role at the junction of carbon and nitrogen assimilation pathways
metabolism
through the enzymatic activity of Gdh2p the breakdown of glutamate provides adequate levels of ammonia in yeast cells. The catabolism of glutamate via the NAD-GDH activity is the major pathway of ammonia generation in vivo. Synthesis of glutamate occurs through the action of NADP-GDH (encoded by GDH1 and GDH3 genes, EC 1.4.1.4). NAD-GDH activity (encoded by GDH2) is responsible for glutamate degradation and release of ammonium and 2-oxoglutarate. The role of GDH1 and GDH2 is contradictory when investigated in yeast strains under cold-growth conditions
metabolism
YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
metabolism
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YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable
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metabolism
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through the enzymatic activity of Gdh2p the breakdown of glutamate provides adequate levels of ammonia in yeast cells. The catabolism of glutamate via the NAD-GDH activity is the major pathway of ammonia generation in vivo. Synthesis of glutamate occurs through the action of NADP-GDH (encoded by GDH1 and GDH3 genes, EC 1.4.1.4). NAD-GDH activity (encoded by GDH2) is responsible for glutamate degradation and release of ammonium and 2-oxoglutarate. The role of GDH1 and GDH2 is contradictory when investigated in yeast strains under cold-growth conditions
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physiological function
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a quantitative genetic study for elucidating the contribution of glutamine synthetase, glutamate dehydrogenase and other nitrogen-related physiological traits to the agronomic performance of common wheat is performed. A total of 148 quantitative trait loci are detected, 26 are detected for GDH activity spread over 13 chromosomes. A coincidence between a quantitative trait loci for GDH activity and a gene encoding GDH is also found on chromosome 2B
physiological function
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GDH enzymes of 19 Streptococcus suis serotype 2 strains, consisting of 18 swine isolates and 1 human clinical isolate from a geographically varied collection, are analyzed by activity staining on a nondenaturing gel. DNA sequences contain base pair differences, but most are silent. Cluster analysis of the deduced amino acid sequences separated the isolates into three groups (ETI, ETII, ETIII). Gene exchange studies results in the change of ETI to ETII and vice versa. A spectrophotometric activity assay for GDH do not show significant differences between the groups
physiological function
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glucose deprivation in SF-188 cells results in an enhanced GDH activity. This results from the loss of glycolysis. Inhibition of Akt signaling, which facilitates glycolysis, increases GDH activity whereas overexpression of Akt suppresses it. Suppression of GDH activity with RNA interference or an inhibitor shows that the enzyme is dispensable in cells able to metabolize glucose but is required for cells to survive impairments of glycolysis brought about by glucose deprivation, 2-deoxyglucose, or Akt inhibition. Inhibition of GDH converts these glutamine-addicted SF-188 cells to glucose-addicted cells
physiological function
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sucrose starvation of lupine embryos leads to a rapid increase in the specific activity of GDH, immunoreactive beta-polypeptide and it is accompanied by appearance of new cathodal isoforms of enzyme, suggesting that isoenzymes induced in lupine embryos by sucrose starvation combine into GDH hexamers with the predominance of beta-GDH subunits synthetized under GDH1 gene control, treatment of cultivated embryos with 0.01 mM Cd2+ or Pb2+ results in ammonium accumulation in the tissues, accompanied by an increase in anabolic activity of GDH and activity of anodal isoenzymes
physiological function
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transgenic mice, betaGlud1-/-, are generated bearing a beta-cell-specific GDH deletion. In situ pancreatic perfusion reveals that glucose-stimulated insulin secretion is reduced by 37% in transgenic mice. Isolated islets with either constitutive or acute adenovirus-mediated knock-out of GDH show a 49 and 38% reduction in glucose-induced insulin release, respectively. Adenovirus-mediated re-expression of GDH in transgenic mice fully restores glucose-induced insulin release. In transgenic mice reduced secretory capacity results in lower plasma insulin levels in response to both feeding and glucose load, while body weight gain is preserved
physiological function
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transgenic tobacco plants overexpressing the two genes encoding the enzyme are generated. Using an in vivo real time 15 N-nuclear magnetic resonance (NMR) spectroscopy approach it is shown that, when the two GDH genes are overexpressed individually or simultaneously, the transgenic plant leaves do not synthesize glutamate in the presence of NH4+ when glutamine synthetase is inhibited. When the two GDH unlabeled substrates ammonium and glutamate are provided simultaneously with either (15N) glutamate or 15NH4+ respectively, it is found that the ammonium released from the deamination of glutamate is reassimilated by the enzyme glutamine synthase, suggesting the occurrence of a futile cycle recycling both ammonium and glutamate
physiological function
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complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites
physiological function
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complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites
physiological function
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CsGDH lacks the regulation by ADP and GTP seen in bovine GDH
physiological function
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Gdh2p plays an evident role during aerobic glutamate metabolism
physiological function
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isozyme GDH7 does not support net amination in vivo and the increase in GDH7 activity might be a response to oxidative stress during protoplast isolation
physiological function
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the main physiological function of NADH-GDH is to provide 2-oxoglutarate for the tricarboxylic acid cycle. Differences in key metabolites of the tricarboxylic acid cycle in the triple mutant versus the wild-type indicate that, through metabolic processes operating mainly in roots, there is a strong impact on amino acid accumulation, in particular alanine, gamma-aminobutyrate, and aspartate in both roots and leaves, phenotypes, overview
physiological function
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a gene disruption mutant fails to produce and secrete glutamate dehydrogenase. In tryptose yeast extract medium, the gluD mutant grows slower than the parent strain. The mutant displys higher sensitivity to H2O2
physiological function
a high-copy number of the GDH2-encoded NADH-specific glutamate dehydrogenase gene stimulates growth at 15°C, while overexpression of NADPH-specific GDH1 has detrimental effects. Total cellular NAD levels are a limiting factor for growth at low temperature in Saccharomyces cerevisiae. Increasing NADH oxidation by overexpression of GDH2 may help to avoid perturbations in the redox metabolism induced by a higher fermentative/oxidative balance at low temperature. Overexpression of GDH2 increases notably the cold growth in the wine yeast strain QA23 in both standard growth medium and synthetic grape must
physiological function
enzyme coordinates metabolism with cell division. Enzymatically active NAD-dependent glutamate dehydrogenase GdhZ directly interferes with FtsZ polymerization by stimulating its GTPase activity, and oxidoreductase-like KidO bound to NADH destabilizes lateral interactions between FtsZ protofilaments. Both GdhZ and KidO share the same regulatory network to concomitantly stimulate the rapid disassembly of the Z-ring, necessary for the subsequent release of progeny cells
physiological function
gene knockout decreases the growth sevenfold and initiates the undecylprodigiosin production in complex Difco nutrient media. With glucose supplementation, the growth difference of the mutant disappears, and significantly increased actinorhodin and undecylprodigiosin biosynthesis can be obtained by limiting the glucose content (0.5 to 1.0%, w/v)
physiological function
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presence of GDH is required for the utilization of glutamate as a major carbon source and to sustain Mycobacterium bovis BCG during infection of both murine RAW 264.7 and bone-marrow derived and macrophages. Inactivation of Gdh increases sensitivity to low pH stress and nitrosative stress
physiological function
silencing of all the endogenous GDH isoform genes leads to a dramatic decrease in total GDH activity but not to any clear morphological or metabolic phenotype in leaves or green fruit. Red fruit on the transgenic plants show markedly reduced levels of Glu and a large increase in aspartate, glucose and fructose content in comparison to wild-type fruit
physiological function
gene YALI0F17820g (GDH1) encodes a NADP-dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NAD-Gdh2 plays a role in nitrogen and carbon utilization from glutamate. GDH1 and GDH2 are not interchangeable
physiological function
glutamate dehydrogenase (GDH) releases ammonia in a reversible NAD(P)+-dependent oxidative deamination of glutamate that yields 2-oxoglutarate (2OG). Plants have distinct isozymes of GDH that are either NAD or NADP-specific. NAD-specific GDHs are localized in mitochondria, whereas NADP-specific GDHs exist in chloroplasts
physiological function
glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NAD-ylGdh2p plays a role in nitrogen and carbon utilization from glutamate. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1, EC 1.4.1.4) or YALI0E09603g (ylGDH2) from Yarrowia lipolytica
physiological function
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in practical water restoration by aquatic plants, the alternative pathway of GDH is more important than the pathway catalyzed by GS in determining the tolerance of submerged macrophytes to high ammonium concentration. Both NADH-dependent and NADPH-dependent GDH (EC 1.4.1.4) show species-dependent variation, in the ammonium-tolerant species, Myriophyllum spicatum, there is a dose-response curve (from 49.46 to 132.99 nmol/min/mg protein for NADH-dependent GDH and 28.98 to 58.67 nmol/min/mg protein for NADPH-GDH), but in the ammonium-sensitive species, Potamogeton lucens, there is little change in activity
physiological function
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in practical water restoration by aquatic plants, the alternative pathway of GDH is more important than the pathway catalyzed by GS in determining the tolerance of submerged macrophytes to high ammonium concentration. Both NADH-dependent and NADPH-dependent GDH (EC 1.4.1.4) show species-dependent variation, in the ammonium-tolerant species, Myriophyllum spicatum, there is a dose-response curve (from 49.46 to 132.99 nmol/min/mg protein for NADH-dependent GDH and 28.98 to 58.67 nmol/min/mg protein for NADPH-GDH), but in the ammonium-sensitive species, Potamogeton lucens, there is little change in activity
physiological function
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the activity of glutamate dehydrogenase in the ammonium-tolerant species Myriophyllum spicatum leaves increases 169% for NADH-dependent GDH and 103% for NADPH-dependent GDH with the [NH4+-N] increasing from 0 to 100 mg/l, performing a dose-response curve while glutamine synthetase activity slightly changes
physiological function
the gdh2/gdh2 mutant is unable to grow on either arginine or proline as a sole carbon and nitrogen source. There is no obvious difference in hyphal development between the wild-type (parental) and the mutant strains when cultured in minimum mineral medium or under other hyphae-inducing conditions. When the gdh2/gdh2 mutant utilizes glucose as the sole carbon source, most of the intracellular metabolites are found at lower concentrations than in the wild-type strain except for cysteine, malonate, nicotinate, 9-heptadecenoate, and 2-phosphoenolpyruvate
physiological function
the NAD-GDH activity in yeast is encoded by GDH2 gene and catalyzes the oxidative deamination of glutamate to 2-oxoglutarate and ammonium. Yeast cells lacking GDH1 can use GDH2 to promote glutamate biosynthesis using ammonia as sole nitrogen source. Role of the GDH path in ROS-mediated apoptosis. GDH2 genetically interacts with GDH3 (EC 1.4.1.4) and controls stress-induced apoptosis. Role of GDH2 in glutamate homeostasis. GDH2 genetically interacts with GDH3 and controls stress-induced apoptosis
physiological function
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a gene disruption mutant fails to produce and secrete glutamate dehydrogenase. In tryptose yeast extract medium, the gluD mutant grows slower than the parent strain. The mutant displys higher sensitivity to H2O2
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physiological function
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gene YALI0F17820g (GDH1) encodes a NADP-dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NAD-Gdh2 plays a role in nitrogen and carbon utilization from glutamate. GDH1 and GDH2 are not interchangeable
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physiological function
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glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NAD-ylGdh2p plays a role in nitrogen and carbon utilization from glutamate. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1, EC 1.4.1.4) or YALI0E09603g (ylGDH2) from Yarrowia lipolytica
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physiological function
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the gdh2/gdh2 mutant is unable to grow on either arginine or proline as a sole carbon and nitrogen source. There is no obvious difference in hyphal development between the wild-type (parental) and the mutant strains when cultured in minimum mineral medium or under other hyphae-inducing conditions. When the gdh2/gdh2 mutant utilizes glucose as the sole carbon source, most of the intracellular metabolites are found at lower concentrations than in the wild-type strain except for cysteine, malonate, nicotinate, 9-heptadecenoate, and 2-phosphoenolpyruvate
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physiological function
-
gene knockout decreases the growth sevenfold and initiates the undecylprodigiosin production in complex Difco nutrient media. With glucose supplementation, the growth difference of the mutant disappears, and significantly increased actinorhodin and undecylprodigiosin biosynthesis can be obtained by limiting the glucose content (0.5 to 1.0%, w/v)
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physiological function
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the NAD-GDH activity in yeast is encoded by GDH2 gene and catalyzes the oxidative deamination of glutamate to 2-oxoglutarate and ammonium. Yeast cells lacking GDH1 can use GDH2 to promote glutamate biosynthesis using ammonia as sole nitrogen source. Role of the GDH path in ROS-mediated apoptosis. GDH2 genetically interacts with GDH3 (EC 1.4.1.4) and controls stress-induced apoptosis. Role of GDH2 in glutamate homeostasis. GDH2 genetically interacts with GDH3 and controls stress-induced apoptosis
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additional information
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at position 242, P6 of the core fingerprint, where NAD+- and NADP+-dependent enzymes normally have Gly or Ala, respectively, clostridial GDH already has Ala. Replacement with Gly produced negligible shift in coenzyme specificity
additional information
each polypeptide consists of an N-terminal substrate-binding (domain I) followed by a C-terminal cofactor-binding segment (domain II). The reaction takes place at the junction of the two domains, which move as rigid bodies and are presumed to narrow the cleft during catalysis. Critical glutamate at the P7 position of the core fingerprint with a role in NAD+ binding, mutational and isothermal titration calorimetry studies, overview
additional information
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each polypeptide consists of an N-terminal substrate-binding (domain I) followed by a C-terminal cofactor-binding segment (domain II). The reaction takes place at the junction of the two domains, which move as rigid bodies and are presumed to narrow the cleft during catalysis. Critical glutamate at the P7 position of the core fingerprint with a role in NAD+ binding, mutational and isothermal titration calorimetry studies, overview
additional information
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GDH from Peptoniphilus asaccharolyticus obeys the rules with Gly at P6 and Glu at P7
additional information
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in clostridial GDH, which shows a remarkable discrimination (20000-80000fold) in favour of NAD+, the P6 residue, which should be Gly, is in fact Ala. Not only this, but the critical P7 residue is Gly instead of Asp or Glu
additional information
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structure-activity relationship, modeling, comparison to other hyperthermophilic enzymes from Pyrococcus furiosus and Thermococcus litoralis, overview
additional information
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the isoenzyme profile in leaves changes on wounding, the change in GDH isoenzyme profile has no effect on ammonium assimilation. Protoplast isolation changes the redox state with NAD(P)H and oxidized glutathione levels increasing, and ascorbate, dehydroascorbate, NAD(P)+ and glutathione decreasing. ATP content in protoplasts declines to 2.6% of that in leaves, while that in wounded leaves increases by twofold
additional information
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the level of GDH alpha- and beta-subunits in tomato plants is regulated differently in each tomato organ
additional information
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the production of monoclonal antibodies against purified glutamate dehydrogenase from Sulfolobus solfataricus is performed with the aim to study the structure-function and evolutionary relationships between various types of glutamate dehydrogenases
additional information
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Trp243 is located in the active-site cleft. Neither Trp64 nor Trp449 are strictly required for pH-dependent inactivation
additional information
several (+/-)-2-methyl-2,4-pentanediol (MPD) binding sites with conserved sequence are identified, but AtGDH1 is insensitive to MPD in activity assays. Structure function analysis of AtGDH1, overview. The open-to-closed conformational transition is required to form a fully functional active site
additional information
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several (+/-)-2-methyl-2,4-pentanediol (MPD) binding sites with conserved sequence are identified, but AtGDH1 is insensitive to MPD in activity assays. Structure function analysis of AtGDH1, overview. The open-to-closed conformational transition is required to form a fully functional active site
additional information
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the level of GDH alpha- and beta-subunits in tomato plants is regulated differently in each tomato organ
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additional information
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the production of monoclonal antibodies against purified glutamate dehydrogenase from Sulfolobus solfataricus is performed with the aim to study the structure-function and evolutionary relationships between various types of glutamate dehydrogenases
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E27F
improved thermostability as compared to wild-type
E27K
slightly improved thermostability as compared to wild-type
E27V
slightly improved thermostability as compared to wild-type
G255A
no significant thermostability
G82K
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dramatically switches to increased specificity for oxaloacetate, 280fold higher than those for 2-oxoglutarate
G82R
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specific activity not drastically altered compared to the wild-type
K80R
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specific activity not drastically altered compared to the wild-type
M101K
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specific activity not drastically altered compared to the wild-type
M101S
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dramatically switches to increased specificity for oxaloacetate, 495fold higher than those for 2-oxoglutarate
Q144C
improved thermostability as compared to wild-type
Q144D
slightly improved thermostability as compared to wild-type
Q144K
no improved thermostability as compared to wild-type
Q144R
highly improved thermostability as compared to wild-type
W100R
no significant thermostability
E27F
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improved thermostability as compared to wild-type
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G255A
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no significant thermostability
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Q144C
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improved thermostability as compared to wild-type
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Q144R
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highly improved thermostability as compared to wild-type
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W100R
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no significant thermostability
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Y187M
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no further stimulation of the mutated GDH isoenzymes by ADP in contrast to the wild-type
C825G
no large changes in catalytic activity
C872R
no large changes in catalytic activity
D869A
no large changes in catalytic activity
D885A
complete loss of activtiy
K810A
complete loss of activtiy
K820A
complete loss of activtiy
R784A
complete loss of activtiy
S1142A
complete loss of activtiy
V1139A
no large changes in catalytic activity
E243R
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the mutation shows reduced activity and almost no discrimination against NADPH compared to NADH
molecular biology
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alpha-ketoglutarate dehydrogenase and GDH play a critical role in modulating alpha-ketoglutarate homeostasis
G376K
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faster thermal inactivation, higher specific activity at 58°C
N97D
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faster thermal inactivation
N97D/G376K
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faster thermal inactivation, higher specific activity at 58°C
A242G
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site-directed mutagenesis, the mutant shows A242G showed a decreased overall catalytic efficiency for NADH at all pH values of pH 6.0-8.0 after Ala replacement with Gly compared to the wild-type enzyme, the mutation had a severe effect on the overall catalytic efficiency with NADPH as coenzyme
D165H
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site-directed mutagenesis, catalytically inactive mutant
D165N
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residual 2% of wild-type activity when purified after expression in Escherichia coli at 37°C, cells induced at 8°C are 1000fold less active than that produced at 37°C, spontaneous deamidation, which depends on the residual catalytic machinery of the mutated GDH active site
D165N/K125A
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correctly folded, no significant deamidation
F187D
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dimeric form of enzyme
F232S/P262S/D263K
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site-directed mutagenesis, the mutant shows switched cofactor spcificity compared to the wild-type enzyme, it has high activity with NADPH/NADP+
F238S/P262S/D263K/N290G
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S/P262S/N290G
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S?P262S?D263K
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site-directed mutagenesis, the mutant shows complete reversal in coenzyme selectivity from NAD(H) to NADP(H) with retention of high levels of catalytic activity for the second coenzyme
N290G
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
C1141T
no large changes in catalytic activity
C1141T
residue C1141 is responsible for the inhibition of enzyme activity by HgCl2, and HgCl2 functions as an activating compound for mutant C1141T
D245K
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the mutation shows reduced activity and 36.4fold discrimination against NADPH compared to NADH
D245K
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site-directed mutagenesis, discrimination against NADPH by factor 32, compared to 1000 for the wild-type enzyme
E243D
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the mutation shows reduced activity and 130fold discrimination against NADPH compared to NADH
E243D
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site-directed mutagenesis, substitution of Asp for Glu in E243D produces a shift in favour of NADPH by virtue of a threefold increase in the Km for NAD+ and a threefold decrease in that for NADP+, resulting in a 9fold shift in the overall discrimination factor, discrimination against NADPH by factor 130, compared to 1000 for the wild-type enzyme
E243D
site-directed mutagenesis, the enzyme shows impaired NADH binding and catalytic activity due to the disruption of hydrogen bonds with 2'-OH and 3'-OH groups of ribose
E243K
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the mutation shows reduced activity and almost no discrimination against NADPH compared to NADH
E243K
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site-directed mutagenesis, discrimination against NADPH by a factor below 130, compared to 1000 for the wild-type enzyme
E243K
site-directed mutagenesis, the enzyme shows highly impaired NADH binding, inability of E243K to effectively switch to NADPH, which may be explained by the position of the P7 side chain, which is not be ideal for binding to the 2'-phosphate
W244S
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the mutation shows reduced activity and 205fold discrimination against NADPH compared to NADH
W244S
site-directed mutagenesis, reduced catalytic activity and altered cofactor specificity, importance of Trp244 is apparent from kinetic studies of W244S
D263K
site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants for NAD+, NADH, and NADPH, but decreased for DTNB leading to inactivation by the inhibitor
D263K
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site-directed mutagenesis, the D263K mutation produces remarkably little change in the kinetic parameters for NADH at pH 6.0-8.0 compared to the wild-type enzyme, with NADPH at all three pH values the kcat for the mutant is much higher than for wild-type GDH, and this factor increases from pH 6.0 to pH 7.0 and pH 8.0
D263K
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S
site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
F238S
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site-directed mutagenesis, the mutant shows markedly increased catalytic efficiency with NADPH, especially at pH 8.0 in the range of pH 6.0-8.0
F238S/P262S
site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
F238S/P262S
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site-directed mutagenesis, the mutant shows altered cofactor specificity compared to the wild-type enzyme
F238S/P262S
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site-directed mutagenesis, the mutant shows markedly increased catalytic efficiency with NADPH, especially at pH 8.0 in the range of pH 6.0-8.0
P262S
site-directed mutagenesis, the mutant shows altered binding kinetics for cofactors compared to the wild-type enzyme, the mutant shows increased dissociation constants
P262S
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site-directed mutagenesis, the mutant shows markedly increased catalytic efficiency with NADPH, especially at pH 8.0 in the range of pH 6.0-8.0
W243F
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decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W243F
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site-directed mutagenesis, catalytically impaired enzyme due to hindered glutamate binding, the mutant shows Michaelis-Menten kinetics
W310F
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more thermostable than the wild type enzyme
W310F
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site-directed mutagenesis, the mutant shows Michaelis-Menten kinetics
W393F
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site-directed mutagenesis
W393F
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increased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W449F
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decreased activity compared to the wild type enzyme, more thermostable than the wild type enzyme
W449F
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site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme
W64F
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65% wild type enzyme activity, less thermostable than the wild type enzyme
W64F
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site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme
additional information
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construction of backcrossed homozygous gdh1, gdh2, gdh3, gdh1-2, and gdh1-2-3 mutants. Enzyme activity in the roots of the gdh1 single mutant is similar to the wild-type, NADH-GDH activity in the roots of the gdh2 mutant is about 25% lower than the wild type, whereas in the roots of the gdh3 mutant, the enzyme activity is 30% higher. In the leaves, there is a 60% reduction in NADH-GDH activity in the gdh1 single mutant but not in the other two single mutants. By contrast, both in the roots and in the leaves of the gdh1-2 double mutant, a dramatic decrease in NADH-GDH activity occurs, butin the gdh1-2 double mutant, some remaining enzyme activity is still detected in the roots. No NADH-GDH enzyme activity is detected in either of the organs of the gdh1-2-3 triple mutant. No NADPH-GDH enzyme activity is detected in the wild type or in the gdh single, double, or triple mutants. Metabolic profiling of the gdh1-2-3 triple mutant, e.g. placed under continuous darkness, overview
additional information
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site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview
additional information
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site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview
additional information
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construction of an enzyme deletion DELTAgdh2 mutant, the mutant shows less than 15-20% of wild-type activity, but DELTAgdh3 shows 20fold increased NAD+-dependent GDH activity, EC 1.4.1.2, genotypes and phenotypes, overview
additional information
YALI0E09603g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
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YALI0E09603g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
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YALI0E09603g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
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additional information
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an active chimera (CEC) consisting of the substrate-binding domain (domain I) of CsGDH and the coenzyme-binding domain (domain II) of Escherichia coli GDH is generated. Kinetic constants of chimeric protein: Km values for substrates L-glutamate, 2-oxoglutarate, NH4Cl highly increased compared to wild-type, Vmax values also highly increased compared to wild-type. The CEC chimera, like Escherichia coli GDH, has a marked preference for NADP(H) as coenzyme. selectivity for the phosphorylated coenzyme does indeed reside solely in domain II. Positive cooperativity toward L-glutamate, characteristic of wild-type CsGDH, retains with domain I. Although glutamate cooperativity occurs only at higher pH values in the wild-tpye CsGDH, the chimeric protein shows it over the full pH range explored. The chimera is capable of catalyzing severalfold higher reaction rates (Vmax) in both directions than either of the parent enzymes from which it is constructed
additional information
chimaeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
additional information
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chimaeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
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drug development
although AtGDH1 is insensitive to MPD in activity assays, several (+/-)-2-methyl-2,4-pentanediol (MPD) binding sites with conserved sequence are identified and the observation of druggable sites opens a potential for non-competitive herbicide design
energy production
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a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride
agriculture
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GDH genes involved in leaf senescence are also a component of the plant defence response during plantpathogen interaction, GDH behaves like a non-specific stress-related gene
agriculture
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plays some role in triticale plants defence against effects of different types of environmental stresses
agriculture
a high-copy number of the GDH2-encoded NADH-specific glutamate dehydrogenase gene stimulates growth at 15°C, while overexpression of NADPH-specific GDH1 has detrimental effects. Total cellular NAD levels are a limiting factor for growth at low temperature in Saccharomyces cerevisiae. Increasing NADH oxidation by overexpression of GDH2 may help to avoid perturbations in the redox metabolism induced by a higher fermentative/oxidative balance at low temperature. Overexpression of GDH2 increases notably the cold growth in the wine yeast strain QA23 in both standard growth medium and synthetic grape must
analysis
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evaluation of the C.Diff Quik Chek Complete Assay which tests for the presence of both glutamate dehydrogenase and toxins A and B. The assay allows 88% of specimens to be accurately screened as either positive or negative for the presence of toxigenic Clostridium difficile in less than 30 min and with minimal hands-on time. Use of a random-access PCR for the analysis of specimens with discrepant allows the easy, rapid, and highly sensitive and specific diagnosis of Clostridium difficile disease
analysis
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gluD gene encoding glutamate dehydrogenase is highly conserved and glutamate dehydrogenase, which is used as marker for the presence of Clostridium difficile in fecal specimens, is readily expressed in vitro by all 77 Clostridium difficile ribotypes assayed. All ribotypes, including ARL 002, ARL 027, and ARL 106, are reactive in assays that detect Clostridium difficile glutamate dehydrogenase
analysis
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the latex test-reactive protein is a glutamate dehydrogenase present in all isolates of Peptoclostridium difficile analyzed, suggesting that it is not related to pathogenicity
analysis
the protein that reacts in commercial latex tests for Clostridium difficile is a glutamate dehydrogenase
biotechnology
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a strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibit faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Flocculation of both Y and Y-5 can be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation is promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. This opens up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing
biotechnology
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method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization
biotechnology
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the rate of flocculation is promoted by a-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing
degradation
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at high salinity glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH, whereas GS-catalysis might be the main glutamate synthesis pathway under low salinity
degradation
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clarification of the in vivo direction of the reaction catalyzed by GDH isoenzyme 1, the enzyme catabolizes L-glutamate in roots, and does not assimilate NH4+ in source leaves
diagnostics
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GDH electrophoretic type (ETs) and sequence types may serve as useful markers in predicting the pathogenic behavior of strains of this serotype and that the molecular basis for the observed differences in the ETs is amino acid substitutions and not deletion, insertion, or processing uniqueness
diagnostics
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GLDH, gama-glutamyltransferase, aspartate-aminotransferase, alanine-aminotransferase and erythrocyte mean cell volume are assessed in 238 alcoholics admitted to hospital: on admission, after 24 h and after 7 days. All the values are significantly higher than those in healthy persons. The fastest activity decrease is seen in GLDH. The kinetics of GLDH and aspartate-aminotranferase are more applicable than gama-glutamyltransferase kinetics after a week, but GLDH kinetics are most reliable. GLDH is the most specific laboratory marker with almost 90% specificity. The sensitivity of combination erythrocyte mean cell volume and GLDH kinetics after 1 week of abstinence is pathognomonic by 97.2%. GLDH is an equally accurate marker of alcoholism in comparison to others
food industry
plays an essential role during postharvest senescence, its expression most likely is controlled by multigenes and regulated either transcriptionally or posttranscriptionally
food industry
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Lactococcus lactis IFPL 953 shows the highest NAD-GDH activity among wild isolates from raw milk cheeses. L. lactis IFPL 953 also demonstrates a remarkable 2-oxoisovalerate decarboxylase activity, which along with its high GDH activity makes the strain particularly useful in enhancing cheese flavour formation
food industry
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Lactococcus lactis IFPL 953 shows the highest NAD-GDH activity among wild isolates from raw milk cheeses. L. lactis IFPL 953 also demonstrates a remarkable 2-oxoisovalerate decarboxylase activity, which along with its high GDH activity makes the strain particularly useful in enhancing cheese flavour formation
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medicine
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prolonged exposure to Corydalis ternata may be one of the ways to regulate glutamate concentration in brain through the activation of GDH
medicine
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the findings emphasize the integration of glucose metabolism, glutamine metabolism, and oncogenic signaling in glioblastoma cells and suggest that exploiting compensatory pathways of glutamine metabolism can improve the efficacy of cancer treatments that impair glucose utilization
medicine
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evaluation of comercially available rapid membrane enzyme immunoassays that use either glutamate dehydrogenase antigen or toxin A and B detection or a combination of both. Sensitivity, specificity, positive predictive values, and negative predictive values are 63.6%, 98.0%, 76.1%, and 96.4%, respectively, for the CD COMPLETE-toxin assay and 75.5%, 97.4%, 72.5%, and 97.8%, respectively, for the VIDAS CDAB assay. In comparison to the enriched Clostridium difficile cultures, the sensitivity, specificity, positive predictive values, and negative predictive values for the CD COMPLETE-GDH assay are 91.0%, 92.4%, 70.5%, and 98.1%, respectively. The CD COMPLETE assay is a reliable method for the diagnosis of Costridium difficile infection and provides greater sensitivity than toxin enzyme immunoassay alone
medicine
-
gluD gene encoding glutamate dehydrogenase is highly conserved and glutamate dehydrogenase, which is used as marker for the presence of Clostridium difficile in fecal specimens, is readily expressed in vitro by all 77 Clostridium difficile ribotypes assayed. All ribotypes, including ARL 002, ARL 027, and ARL 106, are reactive in assays that detect Clostridium difficile glutamate dehydrogenase
medicine
-
the latex test-reactive protein is a glutamate dehydrogenase present in all isolates of Peptoclostridium difficile analyzed, suggesting that it is not related to pathogenicity
molecular biology
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GDH is essential for the full development of the secretory response in beta-cells
molecular biology
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GDH, in conjunction with NADH-glutamte synthase, contributes to the control of leaf glutamate homeostasis, an amino acid that plays a central signaling and metabolic role at the interface of the carbon and nitrogen assimilatory pathways
synthesis
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produktion of L-ornithine in Corynebacterium glutamicum SNK118, by deletion of genes argF, argR, and ncgl2228 to block the degradation of L-ornithine, and overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenases gene from Clostridium saccharobutylicum and glutamate dehydrogenase RocG. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose are achieved by the final strain in a 10-l bioreactor
synthesis
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produktion of L-ornithine in Corynebacterium glutamicum SNK118, by deletion of genes argF, argR, and ncgl2228 to block the degradation of L-ornithine, and overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenases gene from Clostridium saccharobutylicum and glutamate dehydrogenase RocG. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose are achieved by the final strain in a 10-l bioreactor
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additional information
GDH gene expression and translation are apparently subject to complex regulation
additional information
GDH gene expression and translation are apparently subject to complex regulation
additional information
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GDH gene expression and translation are apparently subject to complex regulation
additional information
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glutamine synthetase-GOGAT pathway and GDH play distinct roles in the source-sink nitrogen cycle of tobacco leaves, regardless of leaf age, [15N]ammonium does not depend on GDH
additional information
high sequence similarity to GDH genes from the Bacteroides, GDH is an anabolic enzyme catalysing the assimilation of ammonia by Entodinium caudatum in the rumen, the gene is probably acquired by lateral gene transfer from a ruminal bacterium
additional information
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high sequence similarity to GDH genes from the Bacteroides, GDH is an anabolic enzyme catalysing the assimilation of ammonia by Entodinium caudatum in the rumen, the gene is probably acquired by lateral gene transfer from a ruminal bacterium
additional information
induction of GDH1 and GDH2 transcripts along the root do not coincide with that of NADH-GOGAT expression
additional information
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induction of GDH1 and GDH2 transcripts along the root do not coincide with that of NADH-GOGAT expression
additional information
large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
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large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
additional information
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possible role of enzyme under Hg-stress
additional information
Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
additional information
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Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
additional information
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reactivation of D165N is a consequence of the catalytic chemistry of the enzymes active site
additional information
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shift in GDH cellular compartmentation is important during leaf nitrogen remobilization
additional information
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subunit rearrangement, i.e., a change in the quaternary structure of the hexameric recombinant GDH, is essential for activation of the enzyme
additional information
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Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
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