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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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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
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
118
-
thermal denaturation starts at 110°C and is comp1eted at 118°C
100
-
half-life: 12 h
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
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Robb, F.T.; Park, J.B.; Adams, M.W.W.
Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus
Biochim. Biophys. Acta
1120
267-272
1992
Pyrococcus furiosus
brenda
Diruggiero, J.; Robb, F.T.
Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
Appl. Environ. Microbiol.
61
159-164
1995
Pyrococcus furiosus
brenda
Yip, K.S.; Baker, P.J.; Britton, K.L.; Engel, P.C.; Rice, D.W.; Sedelnikova, S.E.; Stillman, T.J.; Pasquo, A.; Chiaraluce, R.; Consalvi, V.; Scandurra, R.
Crystallization of the NAD(P)-dependent glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus
Acta Crystallogr. Sect. D
51
240-242
1995
Pyrococcus furiosus
brenda
Chiaraluce, R.; Schwerdtfeger, R.M.; Scandurra, R.; Antranikian, G.; Consalvi, V.
Acid-induced disassembly of glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus occurs below pH 2.0
Eur. J. Biochem.
247
224-230
1997
Pyrococcus furiosus (P80319)
brenda
Klump, H.; Di Ruggiero, J.; Kessel, M.; Park, J.B.; Adams, M.W.; Robb, F.T.
Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Thermal denaturation and activation
J. Biol. Chem.
267
22681-22685
1992
Pyrococcus furiosus
brenda
Maras, B.; Valiante, S.; Chiaraluce, R.; Consalvi, V.; Politi, L.; de Rosa, M.; Bossa, F.; Scandurra, R.; Barra, D.
The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium
J. Protein Chem.
13
253-259
1994
Pyrococcus furiosus (P80319)
brenda
Yip, K.S.; Stillman, T.J.; Britton, K.L.; Artymiuk, P.J.; Baker, P.J.; Sedelnikova, S.E.; Engel, P.C., Pasquo, A.; Chiaraluce, R.; Consalvi, V.; et al.
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
Structure
15
1147-1158
1995
Pyrococcus furiosus (P80319)
brenda
Britton, K.; Baker, P.; Borges, K.; Engel, P.; Pasquo, A.; Rice, D.; Robb, F.; Scandurra, R.; Stillman, T.; Yip, K.
Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis
Eur. J. Biochem.
229
688-695
1995
Pyrococcus furiosus (P80319), Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
brenda
Lee, M.; Gonzlez, J.; Robb, F.
Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis Cloning and comparison with two marine hyperthermophilic GDHs
Extremophiles
6
151-159
2002
Pyrococcus furiosus (P80319), Thermococcus litoralis (Q56304), Thermococcus litoralis DSM 5473 (Q56304)
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus (P80319)
brenda