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Literature summary for 1.4.1.3 extracted from

  • 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 (1995), Biochim. Biophys. Acta, 1251, 170-176.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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Renatured (Commentary)

Renatured (Comment) Organism
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 Saccharolobus solfataricus

Subunits

Subunits Comment Organism
monomer 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 Saccharolobus solfataricus
oligomer 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 Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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 Saccharolobus solfataricus