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 | 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 (Comment) | Organism |
---|---|
gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli | Fusarium graminearum |
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 | 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 | 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 | 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 | 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 | 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 | 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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | 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 | ? | - |
? | |
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 | ? | - |
? | |
N-acetyllactosamine + O2 | - |
Fusarium graminearum | ? | - |
? | |
raffinose + O2 | - |
Fusarium graminearum | 6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O | - |
? | |
spruce galactoglucomannan + O2 | - |
Fusarium graminearum | ? | - |
? | |
tamarind galactoxyloglucan + O2 | - |
Fusarium graminearum | ? | - |
? |
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 | Comment | Organism |
---|---|---|
GAO | - |
Fusarium acuminatum |
GAO | - |
Fusarium graminearum |
GAO | - |
Fusarium subglutinans |
GAO | - |
Fusarium verticillioides |
GAO | - |
Fusarium konzum |
GAO | - |
Fusarium thapsinum |
GAO | - |
Fusarium nygamai |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Cys-Tyr cofactor | - |
Fusarium acuminatum | |
Cys-Tyr cofactor | - |
Fusarium graminearum | |
Cys-Tyr cofactor | - |
Fusarium subglutinans | |
Cys-Tyr cofactor | - |
Fusarium verticillioides | |
Cys-Tyr cofactor | - |
Fusarium konzum | |
Cys-Tyr cofactor | - |
Fusarium thapsinum | |
Cys-Tyr cofactor | - |
Fusarium nygamai |
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 |