1.4.1.3: glutamate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about glutamate dehydrogenase [NAD(P)+], go to the full flat file.
Reaction
Synonyms
At5g07440, At5g18170, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), dual-coenzyme specific glutamate dehydrogenase, GDH, gdh-1, GDH1, GDH2, GDH3, GdhA, gdhA_1, GDHB, GDHII, GLDH, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase 1, glutamate dehydrogenase 2, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2, hGLUD1, hGLUD2, housekeeping glutamate dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, Legdh1, Membrane protein 50, MP50, NAD(P)+-dependent glutamate dehydrogenase, NAD(P)-dependent GDH, NAD(P)-dependent glutamate dehydrogenase, NAD(P)-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, NAD(P)H-utilizing glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, TTC1211, TTC1212, TtGDH
ECTree
1.4.1.3 glutamate dehydrogenase [NAD(P)+]Advanced search results
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results (Temperature Stability
Temperature Stability on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+]
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
0
-
complete loss of activity after 5 h, 20% glycerol protects from inactivation
100
100 - 105
-
1 mg/ml enzyme, half-life of 10.5 h at 100°C, 3.5 h at 105°C, and 20 h at 90°C, thermal denaturation at 113°C
104
110
25 - 70
-
the thermostability of the enzyme at neutral pH is very high even at 70°C, but at acidic pH values, the dissociation of enzyme subunits produces the rapid enzyme inactivation even at 25°C, immobilized preparations, as well as the soluble enzyme, remain fully active after 24 h of incubation at 60°C and pH 7, the optimal glyoxyl agarose derivative obtained is fully stable at pH 4 and 25°C, retaining more than 90% of its activity after incubation at 45°C for 24 h at pH 4 and more than 75% of the activity after the same period at 50°C
42
-
mitochondrial enzyme loses 80% activity after 20 min, enzyme from endoplasmic reticulum loses 20% activity
45
47.5
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GDH2 has a half-life of 38 min at 47.5°C, GDH1 has a half-life of 348 min at 47.5°C, high concentrations of phosphate (300 mM) have a protective effect on the thermal denaturation of both wild type hGDHs, this effect being more pronounced for GDH2
60
-
48 h, protein concentration of 0.2 mg/ml, 20% loss of activity
70
70 - 100
-
no loss in activity after 1 h at 90°C, 20% residual activity after 1 h at 100°C
75
80
90
95
-
half-life: 15 min at 0.4 mg/ml, 30 min at 0.8 mg/ml. Temperature-dependent inactivation of the enzyme is irreversible, this process is accompanied by a progressive increase in hydrophobic surface area which leads to protein precipitation
98
half-life: 2 h. alignment of the sequences for the thermophilic glutamate dehydrogenases from Thermococcus litoralis and Pyrococcus furiosus against the sequence and the molecular structure of the glutamate dehydrogenase from the mesophile Clostridium symbiosum provides insights into the molecular basis of their thermostability. A relatively small number of amino acid substitutions is observed between the two thermophilic glutamate dehydrogenase sequences. The most frequent amino acid exchanges involves substitutions which increase the hydrophobicity and sidechain branching in the more thermostable enzyme. Particularly common is the substitution of valine to isoleucine. Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures. One hot spot for the accumulation of exchanges lies close to a region of the molecule involved in its conformational flexibility and these changes may modulate the dynamics of this enzyme and thereby contribute to increased stability
additional information
100
-
half-life: 2.3 h at 0.053 mg/ml protein concentration, 10 h at 1.06 mg/ml protein concentration
100
-
native enzyme, half-life at 100°C: 10.5 h, recombinant enzyme, half-life at 75°C: 7h, at 90°C: 8.1 h
100
half-life: 12 h. alignment of the sequences for the thermophilic glutamate dehydrogenases from Thermococcus litoralis and Pyrococcus furiosus against the sequence and the molecular structure of the glutamate dehydrogenase from the mesophile Clostridium symbiosum provides insights into the molecular basis of their thermostability. A relatively small number of amino acid substitutions is observed between the two thermophilic glutamate dehydrogenase sequences. The most frequent amino acid exchanges involves substitutions which increase the hydrophobicity and sidechain branching in the more thermostable enzyme. Particularly common is the substitution of valine to isoleucine. Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures. One hot spot for the accumulation of exchanges lies close to a region of the molecule involved in its conformational flexibility and these changes may modulate the dynamics of this enzyme and thereby contribute to increased stability
104
half-life: 67 min in absence of KCl, 562 min in presence of 1 M KCl
104
half-life: 4.9 min in absence of KCl, 45 min in presence of 1 M KCl
110
-
thermal denaturation starts at 110°C and is completed at 118°C. The process of heat activation from 40 to 80°C is accompanied by a much smaller increase in absorbance at 280 nm and a reversible increase in heat capacity with DELTAcal = 187 Kcal/mol GDH and Tm = 57°C. This absorbance change as well as the moderate increase in heat capacity suggest that thermal activation leads to some exposure of hydrophobic groups to solvent water as the GDH structure is opened slightly. The increase in absorbance at 280 nm during activation is only 12% of that for denaturation
45
-
half-life of hGDH2 is 45 min in absence of allosteric regulators, hGDH2 is stable for 100 min in presence of 3 mM L-Leu and 1 mM ADP, mutant enzyme hGDH2 S443R has a half life of 300 min
45
-
the half life of isozyme GDH1 is 310 min at 45°C, the half life of isozyme GDH2 is 45 min at 45°C
70
20 min, the activity of the Gdh1/Gdh3 heterohexamers is completely inactivated at 70°C
70
20 min, the activity of the Gdh3 homohexamer and the Gdh1/Gdh3 heterohexamers is completely inactivated at 70°C
75
20 min, the Gdh1homohexamer and the Gdh2/Gdh1 heterohexamers remain active
75
20 min, the Gdh2 homohexamer and the Gdh2/Gdh1 heterohexamers remain active
90
-
incubation for 1 h at 0.2 mg/ml results in 90% loss of activity, incubation for 24 h at 0.8 mg/ml results in 30% loss of activity. Inactivation is irreversible. 3 M guanidine-HCl increases the half-life of the enzyme at 90°C and 0.2 mg/ml 6fold. Half-life at 90°C and 0.2 mg/ml protein concentration increases more than 6fold in the presence of 0.4 M Na2SO4 and decreases 4fold in the presence of 0.4 M NaSCN
additional information
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hGDH1: much slower heat inactivation processes in presence of 1 mM ADP or 3 mM L-Leu
additional information
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much slower heat inactivation processes in presence of 1 mM ADP or 3 mM L-Leu
additional information
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Q441R or S445L mutation makes the enzyme more resistant to thermal inactivation compared to wild-type, K450E or H454Y mutation makes the enzyme extremely heat-labile compared to wild-type
additional information
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at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml. Only the oligomeric form is temperature resistant
additional information
the occurrence of specific substitutions and a possible role for N-epsilon-methylation of lysine residues are discussed in view of current hypotheses on the molecular basis of thermal adaptation of proteins
