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EC Tree
The taxonomic range for the selected organisms is: Saccharolobus solfataricus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hgdh2, glutamate dehydrogenase 1, gdhii, nad(p)-dependent glutamate dehydrogenase, legdh1, nad(p)+-dependent glutamate dehydrogenase, nad(p)-glutamate dehydrogenase, nad(p)h-dependent glutamate dehydrogenase, ttgdh,
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dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))
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glutamic acid dehydrogenase
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glutamic dehydrogenase
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L-glutamate dehydrogenase
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L-glutamic acid dehydrogenase
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Membrane protein 50
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NAD(P)-dependent glutamate dehydrogenase
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NAD(P)-glutamate dehydrogenase
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NAD(P)H-dependent glutamate dehydrogenase
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NAD(P)H-utilizing glutamate dehydrogenase
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reductive amination
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L-glutamate:NAD(P)+ oxidoreductase (deaminating)
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2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
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r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
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r
norvaline + H2O + NADP+
2-oxovalerate + NH3 + NADPH
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activity is 20% of that observed in the presence of 2-oxoglutarate and L-glutamate
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r
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
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2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
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specific activity in the presence of NADH is about 30% of that with NADPH
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H
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highly specific for 2-oxoglutarate and glutamate
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r
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D-glutamate
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2 mM, 11% inhibition, 6 mM, 34% inhibition
o-phthalaldehyde
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0.1 mM, 98% inhibition after 5 min at 60°C, competitive vs. 2-oxoglutarate and NADH
Phenylglyoxal
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4 mM, 75% inhibition, uncompetitive vs. 2-oxoglutarate, noncompetitive vs. NADH
pyridoxal 5'-phosphate
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2 mM, complete loss of activity
additional information
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no inhibition or activation in the presence of ADP, GTP and leucine
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0.063
NAD+
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+ L-glutamate
0.025
NADP+
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+ L-glutamate
0.2
2-oxoglutarate
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cosubstrate NADPH
0.6
2-oxoglutarate
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cosubstrate NADH
1.4
2-oxoglutarate
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pH 7.6, 60°C
0.3
L-glutamate
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cosubstrate NAD+
1.1
L-glutamate
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cosubstrate NADP+
2.5
L-glutamate
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pH 7.6, 60°C
0.007
NADH
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+ 2-oxoglutarate
0.01
NADPH
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+ 2-oxoglutarate
0.01
NADPH
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pH 7.6, 60°C
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0.03 - 0.1
o-phthalaldehyde
0.03
o-phthalaldehyde
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vs. 2-oxoglutarate
0.1
o-phthalaldehyde
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vs. NADH
5
Phenylglyoxal
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vs. 2-oxoglutarate
6
Phenylglyoxal
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vs. NADH
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10
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substrates: L-glutamate + H2O + NADP+
7.6
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NAD(P)H + 2-oxoglutarate + NH3
9
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substrates: 2-oxoglutarate + NH3 + NADPH
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65
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substrates: 2-oxoglutarate + NH3 + NADPH
70
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substrates: L-glutamate + H2O + NADP+
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30 - 90
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30°C: about 90% of activity maximum, 90°C: about 35% of activity maximum
45 - 75
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45°C: about 35% of maximal activity, 75°C: about 20% of maximal activity, substrates: 2-oxoglutarate + NH3 + NADPH
60 - 75
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60°C: about 60% of maximal activity, 75°C: about 30% of maximal activity, substrates: L-glutamate + H2O + NADP+
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5.7
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isoelectric focusing. Microheterogeneity shows three active bands corresponding to pI of 5.7, 5.5 and 5.4. The major band shows an isoelectric point of 5.7
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SwissProt
brenda
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46078
x * 46078, calculated from sequence
44000
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6 * 44000, SDS-PAGE
45000
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6 * 45000, SDS-PAGE
45000
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x * 45000, SDS-PAGE
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?
x * 46078, calculated from sequence
monomer
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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
oligomer
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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
hexamer
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6 * 45000, SDS-PAGE
hexamer
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6 * 44000, SDS-PAGE
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3 - 9
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at least 65% residual activity after 14 h
391621
5.2 - 6.8
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maximal stablility
678367
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25
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48 h, protein concentration of 0.2 mg/ml, stable
60
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48 h, protein concentration of 0.2 mg/ml, 20% loss of activity
70 - 100
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no loss in activity after 1 h at 90°C, 20% residual activity after 1 h at 100°C
95
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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
90
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half-life: 20 min
90
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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
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
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
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guanidine-dependent inactivation of the enzyme at 20°C is irreversible above 1.5 M guanidine hydrochloride
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SDS: 0.1% v/v, no loss of activity after 12 h, 0.5%, half-life 5 h
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urea: 4 M, 10% loss of activity after 12 h, 7.5 M, half-life 9 h
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Ethanol
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50% v/v, complete loss of activity
isopropanol
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50% v/v, complete loss of activity
Methanol
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50% v/v, complete loss of activity
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-20°C, 4°C, 25°C, 6 months, 5% loss of activity
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-70°C, stable for 6 months
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4°C, 1 mg/ml protein concentration, glutamate dehydrogenase remains stable for at least one month
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4°C, 20% loss of activity after 40 days
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4°C, more than 20 days, no loss of activity
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monomeric and oligomeric enzyme show distinct behaviour on guanidine hydrochloride perturbation at neutral pH. The monomer denaturation, although complex, is reversible. Two fluorescent tryptophan classes are detectable in the monomer, monitoring the independent unfolding of two regions through a multistate transition. The oligomeric protein shows a complex denaturation pattern with the tendency to aggregate irreversibly at high denaturant concentration
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Schinkinger, M.F.; Redl, B.; Stffler, G.
Purification and properties of an extreme thermostable glutamate dehydrogenase from the archaebacterium Sulfolobus solfataricus
Biochim. Biophys. Acta
1073
142-148
1991
Saccharolobus solfataricus
brenda
Ahn, J.Y.; Lee, K.S.; Choi, S.Y.; Cho, S.W.
Regulatory properties of glutamate dehydrogenase from Sulfolobus solfataricus
Mol. Cells
10
25-31
2000
Saccharolobus solfataricus
brenda
Consalvi, V.; Chiaraluce, R.; Politi, L.; Pasquo, A.; De Rosa, M.; Scandurra, R.
Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus: studies on thermal and guanidine-dependent inactivation.
Biochim. Biophys. Acta
1202
207-215
1993
Saccharolobus solfataricus
brenda
Consalvi, V.; Chiaraluce, R.; Politi, L.; Gambacorta, A.; De Rosa, M.; Scandurra, R.
Glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.
Eur. J. Biochem.
196
459-467
1991
Saccharolobus solfataricus
brenda
Facchiano, A.M.; Ragone, R.; Consalvi, V.; Scandurra, R.; De Rosa, M.; Colonna, G.
Molecular properties of glutamate dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
Biochim. Biophys. Acta
1251
170-176
1995
Saccharolobus solfataricus
brenda
Maras, B.; Consalvi, V.; Chiaraluce, R.; Politi, L.; De Rosa, M.; Bossa, F.; Scandurra, R.; Barra, D.
The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-epsilon-methyllysine related to thermostability?
Eur. J. Biochem.
203
81-87
1992
Saccharolobus solfataricus (P80053), Saccharolobus solfataricus MT-4 / DSM 5833 (P80053)
brenda