Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.4 extracted from

  • Vuong, T.V.; Foumani, M.; MacCormick, B.; Kwan, R.; Master, E.R.
    Direct comparison of gluco-oligosaccharide oxidase variants and glucose oxidase substrate range and H2O2 stability (2016), Sci. Rep., 6, 37356 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
additional information despite the broad range of applications for glucose oxidase, the effectiveness of glucose oxidase is restricted by the narrow substrate range of this enzyme and susceptibility to H2O2 inactivation Aspergillus niger

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H Aspergillus niger

Inhibitors

Inhibitors Comment Organism Structure
H2O2 loss of 40% activity on D-glucose at 200 mM H2O2 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 Q9HFQ1
-
-

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
-
?
beta-D-glucose + O2 the enzyme is highly specific for D-glucose Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?
additional information the enzyme oxidizes the anomeric carbon of beta-D-glucose using molecular oxygen as an electron acceptor, producing H2O2 and D-glucono-delta-lactone, which in the presence of water spontaneously hydrolyzes to gluconic acid. Poor activity with xylose, maltose, cellobiose, cellotetraose, and xylo-oligosaccharides Aspergillus niger ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Aspergillus niger

Cofactor

Cofactor Comment Organism Structure
FAD a flavoenzyme with a tightly but non-covalently bound FAD cofactor Aspergillus niger

General Information

General Information Comment Organism
evolution glucose oxidase (GO) belongs to the auxiliary activity family AA3_2 Aspergillus niger
malfunction comparison of the substrate profile and H2O2 inactivation of the wild-type glucose oxidase, EC 1.1.3.4, and the Y300A mutant variant of GOOX, the mutant shows a comparatively broad substrate range along with reduced substrate inhibition compared to glucose oxidase, overview Aspergillus niger
additional information narrow binding pocket of glucose oxidase Aspergillus niger