1.1.3.4: glucose oxidase
This is an abbreviated version!
For detailed information about glucose oxidase, go to the full flat file.
Word Map on EC 1.1.3.4
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1.1.3.4
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electrode
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biosensors
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electrochemical
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fabric
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amperometric
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nanoparticles
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film
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gold
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horseradish
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biosensing
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voltammetry
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nanotube
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niger
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electrocatalytic
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biocompatibility
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glassy
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gluconic
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entrap
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hydrogel
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platinum
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nanostructures
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layer-by-layer
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graphene
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electroactive
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nanocomposite
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electrochemistry
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multiwalled
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immunosensors
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co-immobilized
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sol-gel
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polypyrrole
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mesoporous
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prussian
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peroxidase-like
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nafion
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electrodeposition
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ferrocene
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bioelectrocatalytic
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screen-printed
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synthesis
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biocomposite
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diagnostics
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biotechnology
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polyaniline
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biofuel production
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industry
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pharmaceutical industry
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analysis
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metal-organic
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paper-based
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nanozymes
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food industry
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nanosheets
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energy production
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microa
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agriculture
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glucose-responsive
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3,3',5,5'-tetramethylbenzidine
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as-prepared
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photoelectrochemical
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medicine
- 1.1.3.4
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electrode
-
biosensors
-
electrochemical
-
fabric
-
amperometric
- nanoparticles
-
film
- gold
- horseradish
-
biosensing
-
voltammetry
-
nanotube
- niger
-
electrocatalytic
-
biocompatibility
-
glassy
-
gluconic
-
entrap
- hydrogel
- platinum
-
nanostructures
-
layer-by-layer
-
graphene
-
electroactive
-
nanocomposite
-
electrochemistry
-
multiwalled
-
immunosensors
-
co-immobilized
-
sol-gel
-
polypyrrole
-
mesoporous
-
prussian
-
peroxidase-like
-
nafion
-
electrodeposition
- ferrocene
-
bioelectrocatalytic
-
screen-printed
- synthesis
-
biocomposite
- diagnostics
- biotechnology
-
polyaniline
- biofuel production
- industry
- pharmaceutical industry
- analysis
-
metal-organic
-
paper-based
-
nanozymes
- food industry
-
nanosheets
- energy production
-
microa
- agriculture
-
glucose-responsive
- 3,3',5,5'-tetramethylbenzidine
-
as-prepared
-
photoelectrochemical
- medicine
Reaction
Synonyms
AldO, beta-D-glucose oxidase, beta-D-glucose oxygen-1-oxidoreductase, beta-D-glucose/oxygen 1-oxidoreductase, beta-D-glucose: oxygen 1-oxidoreductase, beta-D-glucose:O2 1-oxidoreductase, beta-D-glucose:O2-1-oxidoreductase, beta-D-glucose:oxygen 1-oxido-reductase, beta-D-glucose:oxygen 1-oxidoreductase, beta-D-glucose:oxygen oxidoreductase, beta-D-glucose:oxygen-1-oxidoreductase, beta-D-glucose:quinone oxidoreductase, CngoxA, corylophyline, D-glucose oxidase, D-glucose-1-oxidase, deoxin-1, glucose aerodehydrogenase, glucose oxyhydrase, glucose-1-oxidase, GO-2, GOD, GOX, GOxP5, microcid, More, notatin, oxidase, glucose, pen-GOx, penatin, yGOXpenag
ECTree
1.1.3.4 glucose oxidaseAdvanced search results
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results (General Information
General Information on EC 1.1.3.4 - glucose oxidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
glucose oxidase (GO) belongs to the auxiliary activity family AA3_2
malfunction
physiological function
additional information
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
malfunction
enzyme mutant M12 GOx (N2Y/K13E/T30V/I94V/K152R) shows a 3fold higher activity compared to the wild type at 5 mM glucose and two times higher activity at 200 mM glucose
physiological function
caterpillar labial salivary enzyme glucose oxidase plays an important role in plant-insect interactions by suppressing the caterpillar-induced nicotine production in tobacco plants
physiological function
glucose oxidase (GOx) addition induces the expression and enzymatic activity of manganese peroxidase (MnP) and lignin peroxidase (LiP) from Phanerochaete chrysosporium strain ATCC 24725 cultures. Daily supplementation with GOx-glucose as compared with control cultures causes a remarkable increase in stability of MnP productivity in fungi cultures. Neither H2O2 nor gluconic acid produced by GOx is responsible for improvement of peroxidase activity in nitrogen-limited cultures. GOx increases MnP and LiP activity in the presence of manganese ions
physiological function
glucose oxidase facilitates osteogenic differentiation and mineralization of embryonic stem cells through the activation of nuclear factor (erythroid-derived 2)-like 2, Nrf2, and ERK signal transduction pathways. Glucose oxidase treatment at relatively low concentrations does not change the viability of embryonic stem cells, whereas it enhances osteogenic differentiation and mineralization in the cells. The enzyme induces heme oxygenase-1 and Nrf2 expression via production of H2O2. Glucose oxidase-mediated acceleration of Runx2 expression and mineralization is inhibited either by Nrf2 knockdown or by treating with 5 lM PD98059, an inhibitor of phospho-extracellular signal-regulated kinase (p-ERK). The glucose oxidase-stimulated mineralization is also suppressed by treating the cells with reduced glutathione or catalase, but not by superoxide dismutase or N-acetylcysteine. Viability of the stem cells is not changed by treatment with glucose oxidase within the ranges from 1-10 mU/ml, while it is reduced significantly by adding 20 mU/ml glucose oxidase into the cultures
physiological function
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glucose oxidase from Aspergillus niger shows anti-bacterial activity, but no fungicidal effects
physiological function
glucose oxidase from Penicillium notatum shows no fungicidal effects
physiological function
hydrogen peroxide generated by GOX action has anti-microbial effect
physiological function
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hydrogen peroxide generated by GOX action has anti-microbial effect
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physiological function
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glucose oxidase from Aspergillus niger shows anti-bacterial activity, but no fungicidal effects
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additional information
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424 is a key position for enzyme activity of the immobilized enzyme on electrode surfaces, overview
additional information
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a stable secondary conformation with some degree of freedom at the active sites is essential for the bioelectrocatalytic activity of GOx
additional information
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enzyme denaturing process analysis by molecular dynamics simulations, overview
additional information
enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. Active-site residues of pen-GOx are two histidines, His520 and His563, which act as general base and general acid in the reductive half-reaction and the oxidative half-reaction, respectively
additional information
identification and analysis of structural motifs of the protein which are critical for its stability
additional information
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identification and analysis of structural motifs of the protein which are critical for its stability
additional information
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identification and analysis of structural motifs of the protein which are critical for its stability
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