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Literature summary extracted from

  • Zoldak, G.; Zubrik, A.; Musatov, A.; Stupak, M.; Sedlak, E.
    Irreversible thermal denaturation of glucose oxidase from Aspergillus niger is the transition to the denatured state with residual structure (2004), J. Biol. Chem., 279, 47601-47609.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.3.4 chemical denaturation by 6.67 M guanidine HCl is accompanied by dissociation of the homodimeric enzyme into monomers Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.3.4 thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 additional information
-
thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer Aspergillus niger
1.1.3.4 55.8
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transition temperature is independent of the protein concentration. The thermally denatured enzyme is a compact structure, a form of molten globule-like apoenzyme Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 flavin both the thermal and chemical denaturation of the enzyme cause dissociation of the flavin cofactor Aspergillus niger