Information on EC 1.1.3.5 - hexose oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.3.5
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RECOMMENDED NAME
GeneOntology No.
hexose oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose + O2 = D-glucono-1,5-lactone + H2O2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose phosphate pathway
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
D-hexose:oxygen 1-oxidoreductase
A copper glycoprotein. Also oxidizes D-galactose, D-mannose, maltose, lactose and cellobiose.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-75-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
orange
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Manually annotated by BRENDA team
Citrus vulgaris
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Manually annotated by BRENDA team
red alga
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Manually annotated by BRENDA team
red alga
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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hexose oxidase-mediated hydrogen peroxide is the mechanism for the antibacterial activity, e.g. against Bacillus subtilis strain ATCC 6633, in the red seaweed Ptilophora subcostata. Crude algaeal extract prevents the growth of gram-positive and -negative bacteria, overview, which is completely inhibited by treatment with catalase. But the extract does not affect the growth of either a yeast or a filamentous fungus, such as Candida albicans and Penicillium decambens. The activity is highest in the presence of galactose. Enzyme HOX-mediated H2O2 production represents a defense mechanism against a broad range of bacteria in marine algae
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-galactose + O2
2-deoxy-D-galactono-1,5-lactone + H2O2
show the reaction diagram
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
show the reaction diagram
cellobiose + O2
4-O-(beta-D-glucopyranosido)-D-glucono-1,5-lactone + H2O2
show the reaction diagram
cellobiose + O2
? + H2O2
show the reaction diagram
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?
D-2-glucosamine + O2
2-amine-D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-galactose + O2
D-galacto-1,5-lactone + H2O2
show the reaction diagram
D-galactose + O2
D-galactono-1,5-lactone + H2O2
show the reaction diagram
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-glucose-6-phosphate + O2
D-glucono-1,5-lactone-6-phosphate + H2O2
show the reaction diagram
D-mannose + O2
D-mannono-1,5-lactone + H2O2
show the reaction diagram
D-xylose + O2
D-xylono-1,4-lactone
show the reaction diagram
lactose + O2
4-O-(beta-D-galactopyranosido)-D-glucono-1,5-lactone + H2O2
show the reaction diagram
lactose + O2
? + H2O2
show the reaction diagram
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?
maltose + O2
4-O-(alpha-D-glucopyranosido)-D-glucono-1,5-lactone + H2O2
show the reaction diagram
maltose + O2
? + H2O2
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-galactose + O2
D-galacto-1,5-lactone + H2O2
show the reaction diagram
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?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
additional information
?
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hexose oxidase transforms a number of mono- and oligosaccharides such as beta-D-glucose, D-galactose, xylose, arabinose, cellobiose, lactose, maltose, maltotriose and maltotetraose to corresponding lactones, concomitant with the formation of H2O2, which is used for improving of on rheological and bread making properties of flour, hexose oxidase is used separately in each corn bran-wheat flour formula with L-ascorbic acid at 75 mg/kg, glucose at 0.5% and vital gluten at 9.2%
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
Benzoate
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diethyldithiocarbamate
Galacturonic acids
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glucuronic acid
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hydroxylamine
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propionate
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pyruvate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
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100 mM, 1.5fold increase in activity
NaCl
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20 mM, 1.4fold increase in activity
additional information
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enzyme seems to be activated by proteolytic cleavage of full length protein, remaining polypeptide chains are physically linked together
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.5
cellobiose
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3.8 - 20
D-galactose
2.5 - 8.5
D-glucose
1.7
lactose
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28
maltose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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H2O2 producing activities in different algaeal species, and with different substrates, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 6.3
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6
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broad pH range, two optima can be distinguished
7.2
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87000
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native PAGE on gradient gel
110000
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gel filtration
117000
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gel filtration
130000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 29000 + x * 40000, two bands from purified enzyme in SDS-PAGE, the 29 kDa form seems to be the active/mature enzyme form
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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slow denaturation above
287637
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
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purified native enzyme, pH 7.2, 10 min, completely stable at
50 - 60
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not stable above
60 - 70
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purified native enzyme, pH 7.2, 10 min, 50% activity is retained
80
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purified native enzyme, pH 7.2, 10 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very stable enzyme, no activity decrease after storage at room temperature overnight
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, 7 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-cellulose, Sephadex G-200
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DEAE-Sepharose, Sephacryl S-200, phenyl-Sepharose, chromatofocusing, native and recombinant enzyme
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native enzyme by ammonium sulfate fractionation, followed by anion exchange chromatography and gel filtration
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perfusion chromatography (Poros DEAE-50, Poros HP2, Poros HQ), Sephacryl S200
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Q-Sepharose, Phenyl-sepharose, Superdex 200
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
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recombinant expression in Hansenula polymorpha, i.e. Ogataea angusta
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the purified enzyme HOX is immobilized on graphite electrodes. In the case of direct electronic wiring of HOX, O2 no longer acts as an electron acceptor, and it is the electrode that operates as an electron sink, which may affect the biocatalytic activity of enzymes due to the changed environment/conformation in the active site in the absence of a natural small molecular substrate. The formal potential of FAD in HOX estimated as a mean value of the anodic and cathodic peak potentials is less negative than that of free FAD adsorbed directly onto graphite electrodes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
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the enzyme is useful for improving the rheological and bread making properties of flour and the quality of the bread, overview
nutrition
additional information
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the enzyme is a good candidate for bioelectrochemical applications. Electrochemical study of electron transfer reactions and bioelectrocatalysis of glucose oxidation by enzyme HOX immobilized on graphite electrodes