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Literature summary extracted from

  • Mecheri, B.; De Porcellinis, D.; Campana, P.T.; Rainer, A.; Trombetta, M.; Marletta, A.; Oliveira, O.N.; Licoccia, S.
    Tuning structural changes in glucose oxidase for enzyme fuel cell applications (2015), ACS Appl. Mater. Interfaces, 7, 28311-28318 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.4 additional information the enzyme adopts a stable secondary conformation with some degree of freedom at active sites under acidic-neutral pH values, when either free in solution or immobilized on Nafion. Immobilization on Nafion actually increases the amount of active enzyme (Vmax) and affinity for glucose (inversely proportional to Km) at pH 6.0 Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 additional information
-
 additional information Michaelis-Menten kinetics Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.4 beta-D-glucose + O2 Aspergillus niger
-
 D-glucono-1,5-lactone + H2O2
-
 ?

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.4 commercial preparation
-
 Aspergillus niger
-

Storage Stability

EC Number Storage Stability Organism
1.1.3.4 reaction rate of free GOx in solution remained stable up to 50 days for all investigated pH values, followed by a dramatic decrease owing to enzyme deactivation Aspergillus niger

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.1.3.4 More a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
1.1.3.4 GOX
-
 Aspergillus niger
1.1.3.4 More enzyme type X-S Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD
-
 Aspergillus niger

General Information

EC Number General Information Comment Organism
1.1.3.4 additional information a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx Aspergillus niger