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Literature summary for 1.1.3.4 extracted from

  • Akhtar, M.S.; Ahmad, A.; Bhakuni, V.
    Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer (2002), Biochemistry, 41, 7142-7149.
    View publication on PubMed

General Stability

General Stability Organism
Ca2+ and Mg2+ at 1 M induce compaction of the native conformation of the enzyme, and the enzyme shows a higher stability as compared to the native enzyme against urea denaturation, Ca2+ and Mg2+ at concentrations above 2 M induce dissociation of the native dimeric enzyme, resulting in stabilization of the enzyme monomer, 3 M Ca2+-stabilized monomer retains about 70% secondary structure present in the native enzyme dimer, however there is a complete loss of cooperative interactions between these secondary structural elements present in the enzyme Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Aspergillus niger
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2 + H2O
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Aspergillus niger D-glucono-1,5-lactone + H2O2
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?

Cofactor

Cofactor Comment Organism Structure
FAD
-
Aspergillus niger