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Literature summary for 1.1.3.9 extracted from

  • Parikka, K.; Master, E.; Tenkanen, M.
    Oxidation with galactose oxidase multifunctional enzymatic catalysis (2015), J. Mol. Catal. B, 120, 47-59 .
No PubMed abstract available
Search for more literature for 1.1.3.9

Activating Compound

Activating Compound Comment Organism Structure
copper sulfate
-
 Fusarium acuminatum
copper sulfate
-
 Fusarium graminearum
copper sulfate
-
 Fusarium subglutinans
copper sulfate
-
 Fusarium verticillioides
copper sulfate
-
 Fusarium konzum
copper sulfate
-
 Fusarium thapsinum
copper sulfate
-
 Fusarium nygamai
hexacyanoferrate (III)
-
 Fusarium acuminatum
hexacyanoferrate (III)
-
 Fusarium graminearum
hexacyanoferrate (III)
-
 Fusarium subglutinans
hexacyanoferrate (III)
-
 Fusarium verticillioides
hexacyanoferrate (III)
-
 Fusarium konzum
hexacyanoferrate (III)
-
 Fusarium thapsinum
hexacyanoferrate (III)
-
 Fusarium nygamai
iridium (IV) chloride
-
 Fusarium acuminatum
iridium (IV) chloride
-
 Fusarium graminearum
iridium (IV) chloride
-
 Fusarium subglutinans
iridium (IV) chloride
-
 Fusarium verticillioides
iridium (IV) chloride
-
 Fusarium konzum
iridium (IV) chloride
-
 Fusarium thapsinum
iridium (IV) chloride
-
 Fusarium nygamai
molybdic cyanide
-
 Fusarium acuminatum
molybdic cyanide
-
 Fusarium graminearum
molybdic cyanide
-
 Fusarium subglutinans
molybdic cyanide
-
 Fusarium verticillioides
molybdic cyanide
-
 Fusarium konzum
molybdic cyanide
-
 Fusarium thapsinum
molybdic cyanide
-
 Fusarium nygamai
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
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
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
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
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
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
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
potassium dichromate
-
 Fusarium acuminatum
potassium dichromate
-
 Fusarium graminearum
potassium dichromate
-
 Fusarium subglutinans
potassium dichromate
-
 Fusarium verticillioides
potassium dichromate
-
 Fusarium konzum
potassium dichromate
-
 Fusarium thapsinum
potassium dichromate
-
 Fusarium nygamai
Sodium periodate
-
 Fusarium acuminatum
Sodium periodate
-
 Fusarium graminearum
Sodium periodate
-
 Fusarium subglutinans
Sodium periodate
-
 Fusarium verticillioides
Sodium periodate
-
 Fusarium konzum
Sodium periodate
-
 Fusarium thapsinum
Sodium periodate
-
 Fusarium nygamai

Application

Application Comment Organism
analysis the enzyme can be useful in biosensors Fusarium graminearum
degradation the enzyme can be used for oxygen removal Fusarium graminearum
energy production the enzyme is useful in fuel cells and the usage of biofuel cell with glucose Fusarium graminearum
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)

Cloned (Comment) Organism
gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli Fusarium graminearum

Protein Variants

Protein Variants Comment Organism
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium acuminatum
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium graminearum
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium subglutinans
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium verticillioides
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium konzum
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium thapsinum
additional information engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview Fusarium nygamai

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
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
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
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
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

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Fusarium acuminatum
-
-
extracellular the enzyme is secreted Fusarium graminearum
-
-
extracellular the enzyme is secreted Fusarium subglutinans
-
-
extracellular the enzyme is secreted Fusarium verticillioides
-
-
extracellular the enzyme is secreted Fusarium konzum
-
-
extracellular the enzyme is secreted Fusarium thapsinum
-
-
extracellular the enzyme is secreted Fusarium nygamai
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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
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
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
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-galactose + O2 Fusarium acuminatum
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium graminearum
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium subglutinans
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium verticillioides
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium konzum
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium thapsinum
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium nygamai
-
 D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2 Fusarium verticillioides 7600
-
 D-galacto-hexodialdose + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Fusarium acuminatum
-
-
-
Fusarium graminearum P0CS93 i.e. Gibberella zeae, formerly Dactylium dendroides
-
Fusarium konzum
-
-
-
Fusarium nygamai
-
-
-
Fusarium subglutinans
-
-
-
Fusarium subglutinans A0A0U1YLU5 gene gaoA
-
Fusarium thapsinum
-
-
-
Fusarium verticillioides E6PBN6 gene gaoA
-
Fusarium verticillioides 7600 E6PBN6 gene gaoA
-

Reaction

Reaction Comment Organism Reaction ID
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
a
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
a
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
a
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
a
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
a
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
a
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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Fusarium graminearum ? + H2O2
-
 ?
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 Fusarium acuminatum ? + H2O2
-
 ?
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 Fusarium subglutinans ? + H2O2
-
 ?
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 Fusarium verticillioides ? + H2O2
-
 ?
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 Fusarium konzum ? + H2O2
-
 ?
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 Fusarium thapsinum ? + H2O2
-
 ?
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 Fusarium nygamai ? + H2O2
-
 ?
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 Fusarium graminearum ? + H2O2
-
 ?
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 Fusarium verticillioides 7600 ? + H2O2
-
 ?
2-deoxy-D-galactose + O2
-
 Fusarium graminearum ?
-
 ?
corn arabinoxylan + O2
-
 Fusarium graminearum ?
-
 ?
D-galactose + O2
-
 Fusarium acuminatum D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium graminearum D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium subglutinans D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium verticillioides D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium konzum D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium thapsinum D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium nygamai D-galacto-hexodialdose + H2O2
-
 ?
D-galactose + O2
-
 Fusarium verticillioides 7600 D-galacto-hexodialdose + H2O2
-
 ?
galactoglucomannan + O2
-
 Fusarium graminearum ?
-
 ?
galactoxyloglucan + O2
-
 Fusarium graminearum ?
-
 ?
guar galactomannan + O2
-
 Fusarium graminearum ?
-
 ?
Helix pomatia galactomannan + O2
-
 Fusarium graminearum ?
-
 ?
lactitol + O2
-
 Fusarium graminearum ?
-
 ?
lactobionic acid + O2
-
 Fusarium graminearum ?
-
 ?
lactose + O2
-
 Fusarium graminearum ?
-
 ?
lactulose + O2
-
 Fusarium graminearum ?
-
 ?
lactylamine + O2
-
 Fusarium graminearum ?
-
 ?
larch arabinogalactan + O2
-
 Fusarium graminearum ?
-
 ?
locust bean galactomannan + O2
-
 Fusarium graminearum ?
-
 ?
melibiose + O2
-
 Fusarium graminearum ?
-
 ?
methyl beta-D-mannopyranoside + O2
-
 Fusarium graminearum ?
-
 ?
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 Fusarium acuminatum ?
-
 ?
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 Fusarium subglutinans ?
-
 ?
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 Fusarium verticillioides ?
-
 ?
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 Fusarium konzum ?
-
 ?
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 Fusarium thapsinum ?
-
 ?
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 Fusarium nygamai ?
-
 ?
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 Fusarium graminearum ?
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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 Fusarium verticillioides 7600 ?
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N-acetyllactosamine + O2
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 Fusarium graminearum ?
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raffinose + O2
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 Fusarium graminearum 6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
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spruce galactoglucomannan + O2
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 Fusarium graminearum ?
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tamarind galactoxyloglucan + O2
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 Fusarium graminearum ?
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Subunits

Subunits Comment Organism
monomer 1 * 65000-68000 Fusarium acuminatum
monomer 1 * 65000-68000 Fusarium graminearum
monomer 1 * 65000-68000 Fusarium subglutinans
monomer 1 * 65000-68000 Fusarium verticillioides
monomer 1 * 65000-68000 Fusarium konzum
monomer 1 * 65000-68000 Fusarium thapsinum
monomer 1 * 65000-68000 Fusarium nygamai

Synonyms

Synonyms Comment Organism
GAO
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 Fusarium acuminatum
GAO
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 Fusarium graminearum
GAO
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 Fusarium subglutinans
GAO
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 Fusarium verticillioides
GAO
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 Fusarium konzum
GAO
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 Fusarium thapsinum
GAO
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 Fusarium nygamai

Cofactor

Cofactor Comment Organism Structure
Cys-Tyr cofactor
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 Fusarium acuminatum
Cys-Tyr cofactor
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 Fusarium graminearum
Cys-Tyr cofactor
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 Fusarium subglutinans
Cys-Tyr cofactor
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 Fusarium verticillioides
Cys-Tyr cofactor
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 Fusarium konzum
Cys-Tyr cofactor
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 Fusarium thapsinum
Cys-Tyr cofactor
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 Fusarium nygamai

General Information

General Information Comment Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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