BRENDA - Enzyme Database

Oxidation with galactose oxidase multifunctional enzymatic catalysis

Parikka, K.; Master, E.; Tenkanen, M.; J. Mol. Catal. B 120, 47-59 (2015)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.1.3.9
copper sulfate
-
Fusarium acuminatum
1.1.3.9
copper sulfate
-
Fusarium graminearum
1.1.3.9
copper sulfate
-
Fusarium subglutinans
1.1.3.9
copper sulfate
-
Fusarium verticillioides
1.1.3.9
copper sulfate
-
Fusarium konzum
1.1.3.9
copper sulfate
-
Fusarium thapsinum
1.1.3.9
copper sulfate
-
Fusarium nygamai
1.1.3.9
hexacyanoferrate (III)
-
Fusarium acuminatum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium graminearum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium subglutinans
1.1.3.9
hexacyanoferrate (III)
-
Fusarium verticillioides
1.1.3.9
hexacyanoferrate (III)
-
Fusarium konzum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium thapsinum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium nygamai
1.1.3.9
iridium (IV) chloride
-
Fusarium acuminatum
1.1.3.9
iridium (IV) chloride
-
Fusarium graminearum
1.1.3.9
iridium (IV) chloride
-
Fusarium subglutinans
1.1.3.9
iridium (IV) chloride
-
Fusarium verticillioides
1.1.3.9
iridium (IV) chloride
-
Fusarium konzum
1.1.3.9
iridium (IV) chloride
-
Fusarium thapsinum
1.1.3.9
iridium (IV) chloride
-
Fusarium nygamai
1.1.3.9
molybdic cyanide
-
Fusarium acuminatum
1.1.3.9
molybdic cyanide
-
Fusarium graminearum
1.1.3.9
molybdic cyanide
-
Fusarium subglutinans
1.1.3.9
molybdic cyanide
-
Fusarium verticillioides
1.1.3.9
molybdic cyanide
-
Fusarium konzum
1.1.3.9
molybdic cyanide
-
Fusarium thapsinum
1.1.3.9
molybdic cyanide
-
Fusarium nygamai
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium acuminatum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium graminearum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium subglutinans
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium verticillioides
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium konzum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium thapsinum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium nygamai
1.1.3.9
potassium dichromate
-
Fusarium acuminatum
1.1.3.9
potassium dichromate
-
Fusarium graminearum
1.1.3.9
potassium dichromate
-
Fusarium subglutinans
1.1.3.9
potassium dichromate
-
Fusarium verticillioides
1.1.3.9
potassium dichromate
-
Fusarium konzum
1.1.3.9
potassium dichromate
-
Fusarium thapsinum
1.1.3.9
potassium dichromate
-
Fusarium nygamai
1.1.3.9
Sodium periodate
-
Fusarium acuminatum
1.1.3.9
Sodium periodate
-
Fusarium graminearum
1.1.3.9
Sodium periodate
-
Fusarium subglutinans
1.1.3.9
Sodium periodate
-
Fusarium verticillioides
1.1.3.9
Sodium periodate
-
Fusarium konzum
1.1.3.9
Sodium periodate
-
Fusarium thapsinum
1.1.3.9
Sodium periodate
-
Fusarium nygamai
Application
EC Number
Application
Commentary
Organism
1.1.3.9
analysis
the enzyme can be useful in biosensors
Fusarium graminearum
1.1.3.9
degradation
the enzyme can be used for oxygen removal
Fusarium graminearum
1.1.3.9
energy production
the enzyme is useful in fuel cells and the usage of biofuel cell with glucose
Fusarium graminearum
1.1.3.9
synthesis
the enzyme can be used in the synthesis of small molecules, alcohols or amines, the production of H2O2 and reactive oxygen, and the production of O-glycosylated proteins
Fusarium graminearum
Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.1.3.9
gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli
Fusarium graminearum
Engineering
EC Number
Protein Variants
Commentary
Organism
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium acuminatum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium graminearum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium subglutinans
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium verticillioides
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium konzum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium thapsinum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium nygamai
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium acuminatum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium graminearum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium konzum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium nygamai
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity; high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium subglutinans
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium thapsinum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium verticillioides
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.1.3.9
extracellular
the enzyme is secreted
Fusarium acuminatum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium graminearum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium subglutinans
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium verticillioides
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium konzum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium thapsinum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium nygamai
-
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium acuminatum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium graminearum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium subglutinans
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium verticillioides
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium konzum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium thapsinum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium nygamai
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.1.3.9
D-galactose + O2
Fusarium acuminatum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium graminearum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium subglutinans
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium verticillioides
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium konzum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium thapsinum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium nygamai
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium verticillioides 7600
-
D-galacto-hexodialdose + H2O2
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.1.3.9
Fusarium acuminatum
-
-
-
1.1.3.9
Fusarium graminearum
P0CS93
i.e. Gibberella zeae, formerly Dactylium dendroides
-
1.1.3.9
Fusarium konzum
-
-
-
1.1.3.9
Fusarium nygamai
-
-
-
1.1.3.9
Fusarium subglutinans
-
-
-
1.1.3.9
Fusarium subglutinans
A0A0U1YLU5
gene gaoA
-
1.1.3.9
Fusarium thapsinum
-
-
-
1.1.3.9
Fusarium verticillioides
E6PBN6
gene gaoA
-
1.1.3.9
Fusarium verticillioides 7600
E6PBN6
gene gaoA
-
Reaction
EC Number
Reaction
Commentary
Organism
Reaction ID
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium acuminatum
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium graminearum
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium subglutinans
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium verticillioides
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium konzum
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium thapsinum
1.1.3.9
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
Fusarium nygamai
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.1.3.9
1-methyl-alpha-D-galactopyranoside + O2
in the oxidations of methyl-alpha-D-galactopyranoside and methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium graminearum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium acuminatum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium subglutinans
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium verticillioides
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium konzum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium thapsinum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium nygamai
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidations of methyl-alpha-D-galactopyranoside and methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium graminearum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium verticillioides 7600
? + H2O2
-
-
-
?
1.1.3.9
2-deoxy-D-galactose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
corn arabinoxylan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium acuminatum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium graminearum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium subglutinans
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium verticillioides
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium konzum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium thapsinum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium nygamai
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium verticillioides 7600
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
galactoglucomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
galactoxyloglucan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
guar galactomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
Helix pomatia galactomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactitol + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactobionic acid + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactulose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactylamine + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
larch arabinogalactan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
locust bean galactomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
melibiose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
methyl beta-D-mannopyranoside + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium acuminatum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium subglutinans
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium verticillioides
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium konzum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium thapsinum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium nygamai
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product readily monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium verticillioides 7600
?
-
-
-
?
1.1.3.9
N-acetyllactosamine + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
raffinose + O2
-
743101
Fusarium graminearum
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
?
1.1.3.9
spruce galactoglucomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
tamarind galactoxyloglucan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.1.3.9
monomer
1 * 65000-68000
Fusarium acuminatum
1.1.3.9
monomer
1 * 65000-68000
Fusarium graminearum
1.1.3.9
monomer
1 * 65000-68000
Fusarium subglutinans
1.1.3.9
monomer
1 * 65000-68000
Fusarium verticillioides
1.1.3.9
monomer
1 * 65000-68000
Fusarium konzum
1.1.3.9
monomer
1 * 65000-68000
Fusarium thapsinum
1.1.3.9
monomer
1 * 65000-68000
Fusarium nygamai
Synonyms
EC Number
Synonyms
Commentary
Organism
1.1.3.9
GAO
-
Fusarium acuminatum
1.1.3.9
GAO
-
Fusarium graminearum
1.1.3.9
GAO
-
Fusarium subglutinans
1.1.3.9
GAO
-
Fusarium verticillioides
1.1.3.9
GAO
-
Fusarium konzum
1.1.3.9
GAO
-
Fusarium thapsinum
1.1.3.9
GAO
-
Fusarium nygamai
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.1.3.9
Cys-Tyr cofactor
-
Fusarium acuminatum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium graminearum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium subglutinans
1.1.3.9
Cys-Tyr cofactor
-
Fusarium verticillioides
1.1.3.9
Cys-Tyr cofactor
-
Fusarium konzum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium thapsinum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium nygamai
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.1.3.9
copper sulfate
-
Fusarium acuminatum
1.1.3.9
copper sulfate
-
Fusarium graminearum
1.1.3.9
copper sulfate
-
Fusarium subglutinans
1.1.3.9
copper sulfate
-
Fusarium verticillioides
1.1.3.9
copper sulfate
-
Fusarium konzum
1.1.3.9
copper sulfate
-
Fusarium thapsinum
1.1.3.9
copper sulfate
-
Fusarium nygamai
1.1.3.9
hexacyanoferrate (III)
-
Fusarium acuminatum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium graminearum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium subglutinans
1.1.3.9
hexacyanoferrate (III)
-
Fusarium verticillioides
1.1.3.9
hexacyanoferrate (III)
-
Fusarium konzum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium thapsinum
1.1.3.9
hexacyanoferrate (III)
-
Fusarium nygamai
1.1.3.9
iridium (IV) chloride
-
Fusarium acuminatum
1.1.3.9
iridium (IV) chloride
-
Fusarium graminearum
1.1.3.9
iridium (IV) chloride
-
Fusarium subglutinans
1.1.3.9
iridium (IV) chloride
-
Fusarium verticillioides
1.1.3.9
iridium (IV) chloride
-
Fusarium konzum
1.1.3.9
iridium (IV) chloride
-
Fusarium thapsinum
1.1.3.9
iridium (IV) chloride
-
Fusarium nygamai
1.1.3.9
molybdic cyanide
-
Fusarium acuminatum
1.1.3.9
molybdic cyanide
-
Fusarium graminearum
1.1.3.9
molybdic cyanide
-
Fusarium subglutinans
1.1.3.9
molybdic cyanide
-
Fusarium verticillioides
1.1.3.9
molybdic cyanide
-
Fusarium konzum
1.1.3.9
molybdic cyanide
-
Fusarium thapsinum
1.1.3.9
molybdic cyanide
-
Fusarium nygamai
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium acuminatum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium graminearum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium subglutinans
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium verticillioides
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium konzum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium thapsinum
1.1.3.9
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
Fusarium nygamai
1.1.3.9
potassium dichromate
-
Fusarium acuminatum
1.1.3.9
potassium dichromate
-
Fusarium graminearum
1.1.3.9
potassium dichromate
-
Fusarium subglutinans
1.1.3.9
potassium dichromate
-
Fusarium verticillioides
1.1.3.9
potassium dichromate
-
Fusarium konzum
1.1.3.9
potassium dichromate
-
Fusarium thapsinum
1.1.3.9
potassium dichromate
-
Fusarium nygamai
1.1.3.9
Sodium periodate
-
Fusarium acuminatum
1.1.3.9
Sodium periodate
-
Fusarium graminearum
1.1.3.9
Sodium periodate
-
Fusarium subglutinans
1.1.3.9
Sodium periodate
-
Fusarium verticillioides
1.1.3.9
Sodium periodate
-
Fusarium konzum
1.1.3.9
Sodium periodate
-
Fusarium thapsinum
1.1.3.9
Sodium periodate
-
Fusarium nygamai
Application (protein specific)
EC Number
Application
Commentary
Organism
1.1.3.9
analysis
the enzyme can be useful in biosensors
Fusarium graminearum
1.1.3.9
degradation
the enzyme can be used for oxygen removal
Fusarium graminearum
1.1.3.9
energy production
the enzyme is useful in fuel cells and the usage of biofuel cell with glucose
Fusarium graminearum
1.1.3.9
synthesis
the enzyme can be used in the synthesis of small molecules, alcohols or amines, the production of H2O2 and reactive oxygen, and the production of O-glycosylated proteins
Fusarium graminearum
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.1.3.9
gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli
Fusarium graminearum
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.1.3.9
Cys-Tyr cofactor
-
Fusarium acuminatum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium graminearum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium subglutinans
1.1.3.9
Cys-Tyr cofactor
-
Fusarium verticillioides
1.1.3.9
Cys-Tyr cofactor
-
Fusarium konzum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium thapsinum
1.1.3.9
Cys-Tyr cofactor
-
Fusarium nygamai
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium acuminatum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium graminearum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium subglutinans
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium verticillioides
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium konzum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium thapsinum
1.1.3.9
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
Fusarium nygamai
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium acuminatum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium graminearum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium subglutinans
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium verticillioides
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium konzum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium thapsinum
1.1.3.9
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
Fusarium nygamai
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.1.3.9
extracellular
the enzyme is secreted
Fusarium acuminatum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium graminearum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium subglutinans
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium verticillioides
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium konzum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium thapsinum
-
-
1.1.3.9
extracellular
the enzyme is secreted
Fusarium nygamai
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium acuminatum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium graminearum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium subglutinans
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium verticillioides
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium konzum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium thapsinum
1.1.3.9
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Fusarium nygamai
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.1.3.9
D-galactose + O2
Fusarium acuminatum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium graminearum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium subglutinans
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium verticillioides
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium konzum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium thapsinum
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium nygamai
-
D-galacto-hexodialdose + H2O2
-
-
?
1.1.3.9
D-galactose + O2
Fusarium verticillioides 7600
-
D-galacto-hexodialdose + H2O2
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.1.3.9
1-methyl-alpha-D-galactopyranoside + O2
in the oxidations of methyl-alpha-D-galactopyranoside and methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium graminearum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium acuminatum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium subglutinans
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium verticillioides
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium konzum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium thapsinum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium nygamai
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidations of methyl-alpha-D-galactopyranoside and methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium graminearum
? + H2O2
-
-
-
?
1.1.3.9
1-methyl-beta-D-galactopyranoside + O2
in the oxidation of methyl-beta-D-galactopyranoside, a dimeric product, a water elimination product, and an alpha,beta-unsaturated aldehyde occur among the mix of products. In the case of oxidized beta-galactose, the unsaturated aldehyde likely forms in the reaction
743101
Fusarium verticillioides 7600
? + H2O2
-
-
-
?
1.1.3.9
2-deoxy-D-galactose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
corn arabinoxylan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium acuminatum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium graminearum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium subglutinans
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium verticillioides
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium konzum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium thapsinum
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium nygamai
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
D-galactose + O2
-
743101
Fusarium verticillioides 7600
D-galacto-hexodialdose + H2O2
-
-
-
?
1.1.3.9
galactoglucomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
galactoxyloglucan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
guar galactomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
Helix pomatia galactomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactitol + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactobionic acid + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactulose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
lactylamine + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
larch arabinogalactan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
locust bean galactomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
melibiose + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
methyl beta-D-mannopyranoside + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium acuminatum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium subglutinans
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium verticillioides
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium konzum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium thapsinum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium nygamai
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product readily monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
additional information
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
743101
Fusarium verticillioides 7600
?
-
-
-
?
1.1.3.9
N-acetyllactosamine + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
raffinose + O2
-
743101
Fusarium graminearum
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
?
1.1.3.9
spruce galactoglucomannan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
1.1.3.9
tamarind galactoxyloglucan + O2
-
743101
Fusarium graminearum
?
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.1.3.9
monomer
1 * 65000-68000
Fusarium acuminatum
1.1.3.9
monomer
1 * 65000-68000
Fusarium graminearum
1.1.3.9
monomer
1 * 65000-68000
Fusarium subglutinans
1.1.3.9
monomer
1 * 65000-68000
Fusarium verticillioides
1.1.3.9
monomer
1 * 65000-68000
Fusarium konzum
1.1.3.9
monomer
1 * 65000-68000
Fusarium thapsinum
1.1.3.9
monomer
1 * 65000-68000
Fusarium nygamai
General Information
EC Number
General Information
Commentary
Organism
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium acuminatum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium graminearum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium subglutinans
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium verticillioides
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium konzum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium thapsinum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium nygamai
1.1.3.9
malfunction
deletion of domain 1 completely abolishes the enzyme activity and is thus speculated to be important also for the correct folding of domain 2
Fusarium graminearum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium acuminatum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium graminearum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium subglutinans
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium verticillioides
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium konzum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium thapsinum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium nygamai
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium acuminatum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium graminearum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium subglutinans
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium verticillioides
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium konzum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium thapsinum
1.1.3.9
evolution
galactose oxidases (GAOs) are classified as members of the auxiliary activity (AA) family AA5. This family includes copper radical oxidases and two subfamilies, AA5 1 and AA5 2, containing presently glyoxal oxidases and GAOs, respectively, which share similar tertiary structures and virtually identical active sites despite different catalytic specificities and low sequence similarity
Fusarium nygamai
1.1.3.9
malfunction
deletion of domain 1 completely abolishes the enzyme activity and is thus speculated to be important also for the correct folding of domain 2
Fusarium graminearum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium acuminatum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium graminearum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium subglutinans
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium verticillioides
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium konzum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium thapsinum
1.1.3.9
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
Fusarium nygamai