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

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

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

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

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

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

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

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

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

1.1.3.9

gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli

Fusarium graminearum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium acuminatum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium graminearum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium subglutinans

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium verticillioides

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium konzum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium thapsinum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

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

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

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

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

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

?

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

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

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

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

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

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

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

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

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

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

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

?

?

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

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

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

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

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

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

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

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

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

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

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

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

1.1.3.9

gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli

Fusarium graminearum

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

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium acuminatum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium graminearum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium subglutinans

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium verticillioides

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium konzum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

Fusarium thapsinum

1.1.3.9

engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview

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

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

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

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

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

?

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

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

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

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

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

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

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

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

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

?

?

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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