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Literature summary for 1.1.3.4 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
Search for more literature for 1.1.3.4

Protein Variants

Protein Variants Comment Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Aspergillus niger
-

Storage Stability

Storage Stability Organism
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)

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

Subunits

Subunits Comment Organism
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

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Aspergillus niger

General Information

General Information Comment Organism
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