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BRENDA support

Literature summary for 2.5.1.6 extracted from

  • Iloro, I.; Chehin, R.; Goni, F.M.; Pajares, M.A.; Arrondo, J.L.
    Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study (2004), Biophys. J., 86, 3951-3958.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Subunits

Subunits Comment Organism
More study of thermal unfolding, implications for structure and oligomerization pathway Rattus norvegicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
47 51 Tm-value, irreversible thermal denaturation Rattus norvegicus