1.1.3.9: galactose oxidase
This is an abbreviated version!
For detailed information about galactose oxidase, go to the full flat file.
Word Map on EC 1.1.3.9
-
1.1.3.9
-
neuraminidase
-
copper
-
borohydride
-
lymphocyte
-
lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
-
glycolipids
-
galactosyl
-
glycoconjugates
-
agglutinin
-
nab3h4
-
ganglioside
-
dendroides
-
phenoxyl
-
hydrazide
-
sialylation
-
borotritide
-
graminearum
-
one-electron
-
sialoglycoproteins
-
sialidase
-
galactosamine
-
copper-containing
-
n-acetylgalactosaminyl
-
desialylated
-
naio4
-
synthesis
-
lactoperoxidase
-
galactose-containing
-
degradation
-
diagnostics
-
molecular biology
-
energy production
-
analysis
-
biotechnology
- 1.1.3.9
- neuraminidase
- copper
- borohydride
- lymphocyte
- lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
- glycolipids
-
galactosyl
- glycoconjugates
- agglutinin
-
nab3h4
- ganglioside
- dendroides
-
phenoxyl
- hydrazide
-
sialylation
-
borotritide
- graminearum
-
one-electron
-
sialoglycoproteins
- sialidase
- galactosamine
-
copper-containing
-
n-acetylgalactosaminyl
-
desialylated
- naio4
- synthesis
- lactoperoxidase
-
galactose-containing
- degradation
- diagnostics
- molecular biology
- energy production
- analysis
- biotechnology
Reaction
Synonyms
AOd, At1g14430, At1g19900, At1g67290, At1g75620, At3g53950, At3g57620, At5g19580, beta-galactose oxidase, D-galactose oxidase, F5K20_250, FgrGalOx, galactose 6-oxidase, galactose oxidase, GalOx, GAO, GAOA, GAOX, GLOX1, Glox2, Glox3, GLOX4, GLOX5, GLOX6, GO, GOase, RUBY, RUBY PARTICLES IN MUCILAGE
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Substrates Products
Substrates Products on EC 1.1.3.9 - galactose oxidase
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REACTION DIAGRAM
1-methyl-alpha-D-galactopyranoside + O2
? + H2O2
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
-
-
?
1-O-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
1-O-methyl-D-galactopyranoside + O2
?
-
112% of the activity with D-galactose
-
-
?
2-ethynylglycerol + O2
(2R)-2-ethynylglyceraldehyde + H2O2
-
-
-
?
2-glycerol-alpha-D-galactosylpyranoside + O2
2-glycerol-alpha-D-galactosyl-hexodialdose + H2O2
Polyporus circinatus
-
low activity
-
?
3-chloro-1,2-propanediol + O2
? + H2O2
-
only R isomer will have the correct orientation to react with the enzyme
S isomer
?
4-(methylthio)benzyl alcohol + O2
4-(methylthio)benzaldehyde + H2O2
-
-
-
?
4-(trifluoromethyl)benzyl alcohol + O2
4-(trifluoromethyl)benzaldehyde + H2O2
-
-
-
?
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
5-(hydroxymethyl)furan-2-carbaldehyde + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
?
allyl alcohol + O2
acrolein + H2O2
-
only extracelluar enzyme, low activity
-
?
beta-D-galactopyranosyl-(1-6)-beta-D-galactopyranosyl-(1-4)-D-glucose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
beta-D-galactosyl-(1-6)-beta-D-galactopyranoside + O2
? + H2O2
Polyporus circinatus
-
-
-
?
beta-hydroxypyruvate + O2
2,3-dioxopropionate + H2O2
-
only extracellular enzyme, low activity
-
?
beta-thiogalactoside + O2
beta-thiogalacto-hexodialdose + H2O2
Polyporus circinatus
-
more rapidly oxidized than beta-D-galactose
-
?
ceramide dihexoside + O2
? + H2O2
-
higher activity than free substrate, very low activity as vesicle-bound substrate
-
?
ceramide trihexoside + O2
? + H2O2
-
vesicle-bound and free substrate
-
?
D-Gal-beta-(1-3)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
low activity
-
?
D-Gal-beta-(1-3)-D-Gal-beta-(1-3)-D-Gal-(1-1)-L-Gro + O2
? + H2O2
-
low activity
-
?
D-Gal-beta-(1-3)-D-Gal-beta-(1-6)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
lower activity than with a reversed beta-1-6-linkage
-
?
D-Gal-beta-(1-3)-[D-Gal-beta-(1-6)]-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
best oligosaccharide oxidized
-
?
D-Gal-beta-(1-6)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
faster oxidation than corresponding beta-1-3-linked components
-
?
D-Gal-beta-(1-6)-D-Gal-beta-(1-3)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
improved activity
-
?
D-galactopyranose + ferricyanide
D-galacto-hexodialdose + ferrocyanide
-
ferricyanide poorly replaces O2 as electron acceptor
-
?
D-glucosylpyranoside + O2
D-gluco-hexodialdose + H2O2
-
very low activity
-
?
Forssman glycolipid + O2
? + H2O2
-
higher activity as vesicle-bound substrate, very low activity as free substrate
-
?
Gal-beta-(1-3)-[Fuc-alpha-(1-2)]-GalNAcol + O2
? + H2O2
-
no oxidation of oligosaccharides containing N-acetylgalactosamine at the non-reducing end
-
?
galactan + O2
? + H2O2
-
derived from snail, Lymnea stagnalis galactan best substrate
-
?
galactogen + O2
? + H2O2
-
substrate from Helix pomatia, galactose oxidase acts upon a specific subterminal nonreducing D-galactosyl residue
-
?
globoside + O2
? + H2O2
-
human and porcine globoside, vesicle-bound and free substrate, best substrate tested
-
?
glyceraldehyde + O2
? + H2O2
-
70% of the activity with glycolaldehyde
-
-
?
glycoaldehyde + O2
glyoxal + H2O2
-
only extracellular enzyme, low activity
-
?
hexadecyl-(ethyleneglycol)13-D-galactose + O2
hexadecyl-(ethyleneglycol)13-D-galacto-hexodialdose + H2O2
-
-
-
-
?
hexadecyl-(ethyleneglycol)20-D-galactose + O2
hexadecyl-(ethyleneglycol)20-D-galacto-hexodialdose + H2O2
-
-
-
-
?
hexadecyl-(ethyleneglycol)6-D-galactose + O2
hexadecyl-(ethyleneglycol)6-D-galacto-hexodialdose + H2O2
-
-
-
-
?
hexadecyl-(ethyleneglycol)9-D-galactose + O2
hexadecyl-(ethyleneglycol)9-D-galacto-hexodialdose + H2O2
-
-
-
-
?
isopropyl-beta-D-thiogalactosylpyranoside + O2
isopropyl-beta-D-thiogalactosyl-hexodialdose + H2O2
Polyporus circinatus
-
43% of the activity compared to D-galactose
-
?
methyl alpha-D-galactopyranoside + O2
methyl alpha-D-galacto-hexodialdo-1,5-pyranoside + H2O2
methyl alpha-D-galactopyranoside + O2
methyl alpha-D-galacto-hexodialdose + H2O2
-
-
-
-
?
methyl beta-D-thiogalactosylpyranoside + O2
methyl beta-D-thiogalacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
mucin + O2
? + H2O2
-
bovine submaxillary mucin, native and desialylated
-
?
N-glycolylneuraminic acid + O2
(2R,4S,5R,6R)-2,4-dihydroxy-5-(2-oxoacetamido)-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid + H2O2
N-glycolylneuraminic acid can be selectively oxidized by an engineered variant of galactose oxidase without any reaction toward Neu5Ac. Neu5Gc is also oxidized when it is part of a typical animal oligosaccharide motif and when it is attached to a protein-linked N-glycan
-
-
?
o-nitrophenyl beta-D-galactoside + O2
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
p-nitrophenyl alpha-D-galactoside + O2
1-O-(p-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
-
more reactive than p-nitrophenyl-beta-D-galactoside
-
?
p-nitrophenyl beta-D-galactoside + O2
1-O-(p-nitrophenyl)-beta-D-galactohexodialdose + H2O2
-
less reactive than p-nitrophenyl-alpha-D-galactoside
-
?
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
-
?
1-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
-
?
? + H2O2
-
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
best substrate
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
best substrate
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
high activity
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
high activity
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
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
-
-
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
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
-
-
?
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
?, ir
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
very fast reaction
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
less reactive than nitrophenyl alpha-galactosides
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
unusually large kinetic isotope effect for oxidation of the alpha-deuterated alcohol
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
1-O-methyl-alpha-D-gluco-hexodialdose + H2O2
-
-
-
?
1-O-methyl-alpha-D-glucosylpyranoside + O2
1-O-methyl-alpha-D-gluco-hexodialdose + H2O2
-
very low activity
-
?
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
beta-configuration preferred
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
-
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
less reactive than nitrophenyl alpha-galactosides
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
48% higher activity compared to D-galactose
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
transfer of one electron to O2 in a transition state which is stabilized by a hydrogen bond from the Cu2+-OH2, a rate determining electron transfer that is catalyzed by partial proton transfer
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
one or more tryptophan residues, the Cu(II) atom and the sugar substrate interact within the native enzyme
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
highly active
-
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
highly active
-
?
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
-
-
?
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
-
-
?
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
very low activity
-
?
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
-
?
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
responsible for the conversion of galactosyl residues to the corresponding aldehydes and uronic acids
-
?
2-deoxy-D-galacto-hexodialdose + H2O2
-
-
-
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
-
52% of the activity compared to D-galactose
-
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
-
very low activity
-
?
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
-
i.e. D-cellobiose
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
67% of the activity compared to D-galactose
-
?
beta-D-lacto-hexodialdose + H2O2
-
low activity
-
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
low activity
-
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
high activity
-
?
D-galactosamine + O2
? + H2O2
-
46% of the activity compared to D-galactose
-
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
-
-
-
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
the overall catalytic reaction can be split into two half-reactions, i.e. oxidative and reductive half-reactions
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
two binding sites for D-galactose, highly specific for O2 as electron acceptor
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
high degree of hexose specificity
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
shows also superoxide dismutase activity
-
?
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
150% of the activity with D-galactose
-
-
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
most rapidly oxidized by the same mechanism as for D-galactose
-
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
most rapidly oxidized by the same mechanism as for D-galactose
-
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
best substrate for both intra- and extracellular enzymes
-
?
? + H2O2
Polyporus circinatus
-
bovine brain gangliosides in 70% n-propanol, in aqueous solution not a substrate
-
?
ganglioside + O2
? + H2O2
Polyporus circinatus
-
gangliosides from bovine brain as free molecules and micellar or vesicular dispersions
-
?
(S)-glyceraldehyde + H2O2
-
only extracelluar enzyme, low activity
-
?
glycerol + O2
(S)-glyceraldehyde + H2O2
-
enzyme exhibits prochiral specificity
-
?
glyoxal + H2O2
-
-
approximately 35 mM of glyoxal is produced from 85 mM glycolaldehyde after 7 d of incubation at 50°C and pH 5.5
-
?
melibiose + O2
? + H2O2
high catalytic efficiency
-
-
?
methyl alpha-D-galacto-hexodialdo-1,5-pyranoside + H2O2
-
investigation of the optimal reaction conditions (reaction medium, temperature, concentration and combinations of galactose oxidase, catalase, and horseradish peroxidase are used as variables) to degrade methyl alpha-D-galactopyranoside to alpha-D-galacto-hexodialdo-1,5-pyranoside and thereby reduce byproduct formation. Optimal combination of the 3 enzymes gives methyl alpha-D-galacto-hexodialdo-1,5-pyranoside in approximately 90% yield
-
-
?
methyl alpha-D-galactopyranoside + O2
methyl alpha-D-galacto-hexodialdo-1,5-pyranoside + H2O2
-
-
-
?
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
-
-
-
?
o-nitrophenyl beta-D-galactoside + O2
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
-
ortho-isomer 3 times more potent than para- and meso-forms, 14% of the activity compared to D-galactose
-
?
o-nitrophenyl beta-D-galactoside + O2
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
Polyporus circinatus
-
low activity
-
?
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
-
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
?
? + H2O2
-
more rapidly oxidized than D-galactose
-
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
more rapidly oxidized than D-galactose
-
?
stachyose + O2
? + H2O2
-
oligosaccharides containing D-galactose at the nonreducing end are oxidized by the same mechanism as D-galactose
-
?
?
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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
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additional information
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generation and identification of functional models for GOase based on peptide ligand libraries, combinatorial method, low-molecular-weight model systems for GOase, overview
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additional information
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substrate specificity, no or poor activity with lactose, D-glucose, and guar gum, overview
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additional information
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the enzyme shows broad primary alcohol substrate specificity
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benzyl alcohol is also a substrate for the enzyme
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additional information
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benzyl alcohol is also a substrate for the enzyme
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additional information
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galactose oxidase (GaO) selectively oxidizes the primary hydroxyl of galactose to a carbonyl, facilitating targeted chemical derivatization of galactose-containing polysaccharides, leading to renewable polymers with tailored physical and chemical properties. The activity of wild-type GaO and GaO fusions is measured using the chromogenic ABTS (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid)) assay
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additional information
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galactose oxidase (GaO) selectively oxidizes the primary hydroxyl of galactose to a carbonyl, facilitating targeted chemical derivatization of galactose-containing polysaccharides, leading to renewable polymers with tailored physical and chemical properties. The activity of wild-type GaO and GaO fusions is measured using the chromogenic ABTS (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid)) assay
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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GalOx catalyzes the oxidation of primary alcohols (e.g. the hydroxyl group at the C6 position in D-galactose) to aldehydes, accompanied by the reduction of molecular oxygen to hydrogen peroxide, and shows a broad substrate tolerance, yet strict stereospecificity, for various alcohol substrates. Because of the high sensitivity of GalOx to the stereo configuration of the C4 hydroxyl group D-glucose is not a substrate for the enzyme
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additional information
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GalOx catalyzes the oxidation of primary alcohols (e.g. the hydroxyl group at the C6 position in D-galactose) to aldehydes, accompanied by the reduction of molecular oxygen to hydrogen peroxide, and shows a broad substrate tolerance, yet strict stereospecificity, for various alcohol substrates. Because of the high sensitivity of GalOx to the stereo configuration of the C4 hydroxyl group D-glucose is not a substrate for the enzyme
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additional information
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GalOx catalyzes the oxidation of primary alcohols (e.g. the hydroxyl group at the C6 position in D-galactose) to aldehydes, accompanied by the reduction of molecular oxygen to hydrogen peroxide, and shows a broad substrate tolerance, yet strict stereospecificity, for various alcohol substrates. Because of the high sensitivity of GalOx to the stereo configuration of the C4 hydroxyl group D-glucose is not a substrate for the enzyme
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additional information
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standard ABTS assay. The enzyme is highly specific for molecular oxygen as an electron acceptor, and shows no appreciable activity with a range of alternative acceptors investigated, no activity with ABTS cation radical, ferrocenium ion, 1,4-benzoquinone, 2,6-dichloro-indophenol (DCIP), ferricyanide, guaiacol radical, 2,6-dimethoxyphenol radical, caffeic acid radical, p-coumaric acid radical, ferulic acid radical, sinapic acid radical, thioflavin T, 2-(4'-methylaminophenyl)benzothiazole and 1,10-diethyl-2,20-carbocyanine iodide
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additional information
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standard ABTS assay. The enzyme is highly specific for molecular oxygen as an electron acceptor, and shows no appreciable activity with a range of alternative acceptors investigated, no activity with ABTS cation radical, ferrocenium ion, 1,4-benzoquinone, 2,6-dichloro-indophenol (DCIP), ferricyanide, guaiacol radical, 2,6-dimethoxyphenol radical, caffeic acid radical, p-coumaric acid radical, ferulic acid radical, sinapic acid radical, thioflavin T, 2-(4'-methylaminophenyl)benzothiazole and 1,10-diethyl-2,20-carbocyanine iodide
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additional information
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standard ABTS assay. The enzyme is highly specific for molecular oxygen as an electron acceptor, and shows no appreciable activity with a range of alternative acceptors investigated, no activity with ABTS cation radical, ferrocenium ion, 1,4-benzoquinone, 2,6-dichloro-indophenol (DCIP), ferricyanide, guaiacol radical, 2,6-dimethoxyphenol radical, caffeic acid radical, p-coumaric acid radical, ferulic acid radical, sinapic acid radical, thioflavin T, 2-(4'-methylaminophenyl)benzothiazole and 1,10-diethyl-2,20-carbocyanine iodide
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additional information
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the enzyme is highly selective for galactose and talose but will not oxidize other sugars commonly found on glycoproteins. It oxidizes galactose residues as either monosaccharides or glycoconjugates that contain galactose at the nonreducing end, GC-MS analysis, overview
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additional information
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the enzyme naturally catalyzes the oxidation of the C6 hydroxyl group of D-galactose to the corresponding aldehyde, while simultaneously reducing molecular oxygen to hydrogen peroxide
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additional information
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galactose oxidase catalyzes oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones, respectively. For this purpose, GOase requires a number of additives to sustain its catalytic function, such as the enzyme catalase for degradation of the byproduct hydrogen peroxide as well as single-electron oxidants to reactivate the enzyme upon loss of the amino acid radical in its active site. The substrate specificity of wild-type GOase is rather restricted, it accepts galactose-containing polysaccharides and also some primary alcohols such as dihydroxyacetone and benzyl alcohol
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additional information
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the enzyme naturally catalyzes the oxidation of the C6 hydroxyl group of D-galactose to the corresponding aldehyde, while simultaneously reducing molecular oxygen to hydrogen peroxide
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additional information
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galactose oxidase catalyzes oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones, respectively. For this purpose, GOase requires a number of additives to sustain its catalytic function, such as the enzyme catalase for degradation of the byproduct hydrogen peroxide as well as single-electron oxidants to reactivate the enzyme upon loss of the amino acid radical in its active site. The substrate specificity of wild-type GOase is rather restricted, it accepts galactose-containing polysaccharides and also some primary alcohols such as dihydroxyacetone and benzyl alcohol
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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affinity of enzyme for amphiphiles with larger ethyleneglycol spacer is much larger than for free D-galactose and beta-D-galactopyranosides
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additional information
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more than 95% selectivity for pro-S hydrogen abstraction
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the oxidized form of the enzyme catalyzes the two-electron oxidation of a broad range of primary alcohols to corresponding aldehydes with the concomitant reduction of O2 to H2O2
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the recombinant alcohol oxidase also exhibits aldehyde alcohol oxidase activity and superoxide dismutase activity
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additional information
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no activity with methanol, ethanol, 1-propanol, 1-butanol, 2-propanol, 2-butanol, 2-methoxyethanol, 1,2-propanediol, 1,3-propanediol, glycerol, glyoxylic acid, D-arabinose, D-ribose, D-lyxose, isobutyraldehyde, valeraldehyde, methylglyoxal, benzaldehyde
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