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Literature summary extracted from

  • 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? (1992), Eur. J. Biochem., 203, 81-87.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.3 46078
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x * 46078, calculated from sequence Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Saccharolobus solfataricus P80053
-
-
1.4.1.3 Saccharolobus solfataricus MT-4 / DSM 5833 P80053
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-

Subunits

EC Number Subunits Comment Organism
1.4.1.3 ? x * 46078, calculated from sequence Saccharolobus solfataricus

Temperature Stability [°C]

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