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(furan-2-yl)methanol + O2
furan-2-carbaldehyde + H2O2
-
-
-
?
1,5-anhydrogalactitol + O2
? + H2O2
Polyporus circinatus
-
-
-
?
1-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
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-methyl-beta-D-galactopyranoside + O2
? + H2O2
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-alpha-D-glucosylpyranoside + O2
1-O-methyl-alpha-D-gluco-hexodialdose + H2O2
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
1-O-methyl-D-galactopyranoside + O2
?
-
112% of the activity with D-galactose
-
-
?
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
2-deoxy-D-galactose + O2
?
-
-
-
?
2-ethynylglycerol + O2
(2R)-2-ethynylglyceraldehyde + H2O2
-
-
-
?
2-glycerol-alpha-D-galactosylpyranoside + O2
2-glycerol-alpha-D-galactosyl-hexodialdose + H2O2
Polyporus circinatus
-
low activity
-
?
2-methylene-1,3-propanediol + O2
?
-
-
-
?
3-bromo-1,2-propanediol + O2
? + H2O2
-
-
S isomer
?
3-bromobenzyl alcohol + O2
3-bromobenzaldehyde + H2O2
-
-
-
?
3-chloro-1,2-propanediol + O2
? + H2O2
-
only R isomer will have the correct orientation to react with the enzyme
S isomer
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
-
-
-
?
3-fluoro-1-phenylethanol + O2
?
-
-
-
-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
-
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
?
3-methoxybenzyl alcohol + O2
? + H2O2
-
-
-
-
?
3-nitrobenzyl alcohol + O2
3-nitrobenzaldehyde + H2O2
-
-
-
?
4-(methylthio)benzyl alcohol + O2
4-(methylthio)benzaldehyde + H2O2
-
-
-
?
4-(trifluoromethyl)benzyl alcohol + O2
4-(trifluoromethyl)benzaldehyde + H2O2
-
-
-
?
4-bromobenzyl alcohol + O2
4-bromobenzaldehyde + H2O2
-
-
-
?
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
-
-
-
?
4-fluorobenzyl alcohol + O2
4-fluorobenzaldehyde + H2O2
-
-
-
?
4-iodobenzyl alcohol + O2
4-iodobenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
? + H2O2
-
-
-
-
?
4-methylbenzyl alcohol + O2
4-methylbenzaldehyde + H2O2
-
-
-
?
4-nitrobenzyl alcohol + O2
4-nitrobenzaldehyde + H2O2
-
-
-
?
4-nitrobenzyl alcohol + O2
? + 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
-
-
-
?
acetol + O2
pyruvaldehyde + H2O2
-
-
-
?
allyl alcohol + O2
acrolein + H2O2
-
only extracelluar enzyme, low activity
-
?
alpha-D-melibiose + O2
? + H2O2
-
-
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
benzene-1,2-diamine + O2
? + H2O2
-
very low activity
-
?
benzyl alcohol + O2
? + H2O2
benzyl alcohol + O2
benzaldehyde + H2O2
benzylalcohol + O2
benzaldehyde + H2O2
-
substrate reaction profiling
-
-
?
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-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
beta-hydroxypyruvate + O2
2,3-dioxopropionate + H2O2
-
only extracellular enzyme, low activity
-
?
beta-thiodigalactoside + O2
? + H2O2
Polyporus circinatus
-
-
-
?
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
-
?
corn arabinoxylan + O2
?
-
-
-
?
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-galactosamine + O2
? + H2O2
D-galactose + O2
D-galacto-hexodialdose + H2O2
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
D-glucosylpyranoside + O2
D-gluco-hexodialdose + H2O2
-
very low activity
-
?
D-raffinose + O2
? + H2O2
-
-
-
?
D-xylose + O2
? + H2O2
-
very low activity
-
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
dihydroxyacetone + O2
?
-
-
-
-
?
fetuin + O2
? + H2O2
-
bovine fetuin, native or desialylated
-
?
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
-
?
galactoglucomannan + O2
?
-
-
-
?
galactolipid + O2
? + H2O2
-
-
-
?
galactose 1-phosphate + O2
? + H2O2
Polyporus circinatus
-
very low activity
-
?
galactose-4-SO3Na + O2
? + H2O2
-
very low activity
-
?
galactose-6-SO3Na + O2
? + H2O2
-
very low activity
-
?
galactoxyloglucan + O2
?
-
-
-
?
ganglioside + O2
? + H2O2
globoside + O2
? + H2O2
-
human and porcine globoside, vesicle-bound and free substrate, best substrate tested
-
?
glyceraldehyde + O2
? + H2O2
-
70% of the activity with glycolaldehyde
-
-
?
glycerol + O2
(S)-glyceraldehyde + H2O2
glycoaldehyde + O2
glyoxal + H2O2
-
only extracellular enzyme, low activity
-
?
glycolaldehyde + O2
glyoxal + H2O2
glycolamide + O2
? + H2O2
-
-
-
?
glycoprotein + O2
? + H2O2
-
-
-
?
guar galactomannan + O2
?
-
-
-
?
guar gum + O2
? + H2O2
-
significant activity
-
?
Helix pomatia galactomannan + O2
?
-
-
-
?
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
-
?
L-glucose + O2
L-gluco-hexodialdose + H2O2
-
very low activity
-
?
lactobionic acid + O2
?
-
-
-
?
lactylamine + O2
?
-
-
-
?
larch arabinogalactan + O2
?
-
-
-
?
locust bean galactomannan + O2
?
-
-
-
?
maltose + O2
? + H2O2
-
very low activity
-
?
melibiitol + O2
? + H2O2
Polyporus circinatus
-
-
-
?
melibionic acid + O2
? + H2O2
Polyporus circinatus
-
low activity
-
?
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-mannopyranoside + O2
?
-
-
-
?
methyl beta-D-thiogalactosylpyranoside + O2
methyl beta-D-thiogalacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
mucin + O2
? + H2O2
-
bovine submaxillary mucin, native and desialylated
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
N-acetyllactosamine + O2
?
-
-
-
?
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
-
?
planteose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
sphingoglycolipid + O2
? + H2O2
-
-
-
?
spruce galactoglucomannan + O2
?
-
-
-
?
sucrose + O2
? + H2O2
-
very low activity
-
?
talose + O2
? + H2O2
-
-
-
-
?
tamarind galactoxyloglucan + O2
?
-
-
-
?
xyloglucan + O2
? + H2O2
-
-
-
?
additional information
?
-
1-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
-
?
1-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
-
-
-
?
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 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-galactosylpyranoside + O2
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-glucosylpyranoside + O2
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-galactosylpyranoside + O2
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-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
-
-
-
?
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
very low activity
-
?
2 raffinose + 2 O2
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-galactose + O2
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-glucose + O2
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
-
-
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
67% of the activity compared to D-galactose
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
benzyl alcohol + O2
? + H2O2
-
-
-
-
?
benzyl alcohol + O2
? + H2O2
-
-
-
-
?
benzyl alcohol + O2
? + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
beta-D-lactose + O2
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
-
low activity
-
?
D-galactosamine + O2
? + H2O2
-
-
-
?
D-galactosamine + O2
? + H2O2
-
46% of the activity compared to D-galactose
-
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
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
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
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
-
?
dihydroxyacetone + O2
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
-
?
ganglioside + O2
? + 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
-
?
glycerol + O2
(S)-glyceraldehyde + H2O2
-
only extracelluar enzyme, low activity
-
?
glycerol + O2
(S)-glyceraldehyde + H2O2
-
enzyme exhibits prochiral specificity
-
?
glycolaldehyde + O2
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
-
?
glycolaldehyde + O2
glyoxal + H2O2
-
-
-
-
?
guar + O2
? + H2O2
-
-
-
-
?
guar + O2
? + H2O2
-
-
-
-
?
guaran + O2
? + H2O2
-
only intracellular enzyme
-
?
guaran + O2
? + H2O2
Polyporus circinatus
-
-
-
?
guaran + O2
? + H2O2
Polyporus circinatus
-
highly active
-
?
lactose + O2
?
-
4% of the activity with D-galactose
-
-
?
lactose + O2
? + H2O2
-
-
-
?
lactose + O2
? + H2O2
-
-
-
?
lactose + O2
? + H2O2
Polyporus circinatus
-
very low activity
-
?
melibiose + O2
?
-
103% of the activity with D-galactose
-
-
?
melibiose + O2
? + H2O2
-
-
-
?
melibiose + O2
? + H2O2
high catalytic efficiency
-
-
?
melibiose + O2
? + H2O2
high catalytic efficiency
-
-
?
melibiose + O2
? + H2O2
-
-
-
?
melibiose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
melibiose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
methyl alpha-D-galactopyranoside + O2
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
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
o-nitrophenyl beta-D-galactoside + O2
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
-
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
-
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
?
raffinose + O2
?
-
134% of the activity with D-galactose
-
-
?
raffinose + O2
?
-
-
-
-
?
raffinose + O2
? + H2O2
-
more rapidly oxidized than D-galactose
-
?
raffinose + O2
? + H2O2
-
-
-
?
raffinose + O2
? + H2O2
-
same activity as for D-galactose
-
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
more rapidly oxidized than D-galactose
-
?
stachyose + O2
? + H2O2
-
-
-
?
stachyose + O2
? + H2O2
-
oligosaccharides containing D-galactose at the nonreducing end are oxidized by the same mechanism as D-galactose
-
?
stachyose + O2
? + H2O2
-
only intracellular enzyme
-
?
stachyose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
stachyose + O2
? + H2O2
Polyporus circinatus
-
best substrate tested
-
?
additional information
?
-
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
-
generation and identification of functional models for GOase based on peptide ligand libraries, combinatorial method, low-molecular-weight model systems for GOase, overview
-
-
?
additional information
?
-
-
substrate specificity, no or poor activity with lactose, D-glucose, and guar gum, overview
-
-
?
additional information
?
-
-
the enzyme shows broad primary alcohol substrate specificity
-
-
?
additional information
?
-
benzyl alcohol is also a substrate for the enzyme
-
-
?
additional information
?
-
-
benzyl alcohol is also a substrate for the enzyme
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product readily monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no substrate: D-glucose
-
-
-
additional information
?
-
-
no substrate: D-glucose
-
-
-
additional information
?
-
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The catalytic reaction of GAO comprises oxidative and reductive half-reactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide. During these reactions, the enzyme alters between three different forms: an active, inactive, and fully reduced form. In the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form. Formation of side products in the GAO-catalyzed oxidation, and oxidation of polysaccharides to aldehydes, overview. Aldehydes produced through GAO oxidation of mono- and oligosaccharides can be further oxidized to corresponding uronic acids. The formation of H2O2 in GAO-catalyzed oxidations has enabled substrate screening using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]. In this case, H2O2, produced upon GAO oxidation of galactose or different galactose derivatives, is consumed by horseradish peroxidase during oxidization of ABTS, forming a chromogenic product monitored by spectrophotometric techniques. Product determination and identification by NMR spectroscopy or gas chromatography
-
-
?
additional information
?
-
-
affinity of enzyme for amphiphiles with larger ethyleneglycol spacer is much larger than for free D-galactose and beta-D-galactopyranosides
-
-
?
additional information
?
-
-
more than 95% selectivity for pro-S hydrogen abstraction
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the recombinant alcohol oxidase also exhibits aldehyde alcohol oxidase activity and superoxide dismutase activity
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
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-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
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-galactosamine + O2
? + H2O2
D-galactose + O2
D-galacto-hexodialdose + H2O2
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
D-glucosylpyranoside + O2
D-gluco-hexodialdose + H2O2
-
very low activity
-
?
D-xylose + O2
? + H2O2
-
very low activity
-
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
fetuin + O2
? + H2O2
-
bovine fetuin, native or desialylated
-
?
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
-
?
galactolipid + O2
? + H2O2
-
-
-
?
ganglioside + O2
? + H2O2
globoside + O2
? + H2O2
-
human and porcine globoside, vesicle-bound and free substrate, best substrate tested
-
?
glycoprotein + O2
? + H2O2
-
-
-
?
guar gum + O2
? + H2O2
-
significant activity
-
?
maltose + O2
? + H2O2
-
very low activity
-
?
mucin + O2
? + H2O2
-
bovine submaxillary mucin, native and desialylated
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
planteose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
sphingoglycolipid + O2
? + H2O2
-
-
-
?
sucrose + O2
? + H2O2
-
very low activity
-
?
additional information
?
-
2 raffinose + 2 O2
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-galactose + O2
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-glucose + O2
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
-
-
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
67% of the activity compared to D-galactose
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
beta-D-lactose + O2
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
-
low activity
-
?
D-galactosamine + O2
? + H2O2
-
-
-
?
D-galactosamine + O2
? + H2O2
-
46% of the activity compared to D-galactose
-
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
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
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
-
-
?
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
-
?
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
-
?
ganglioside + O2
? + 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
-
?
guaran + O2
? + H2O2
-
only intracellular enzyme
-
?
guaran + O2
? + H2O2
Polyporus circinatus
-
-
-
?
guaran + O2
? + H2O2
Polyporus circinatus
-
highly active
-
?
melibiose + O2
? + H2O2
-
-
-
?
melibiose + O2
? + H2O2
-
-
-
?
melibiose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
melibiose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
-
-
?
raffinose + O2
? + H2O2
-
more rapidly oxidized than D-galactose
-
?
raffinose + O2
? + H2O2
-
-
-
?
raffinose + O2
? + H2O2
-
same activity as for D-galactose
-
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
more rapidly oxidized than D-galactose
-
?
stachyose + O2
? + H2O2
-
-
-
?
stachyose + O2
? + H2O2
-
oligosaccharides containing D-galactose at the nonreducing end are oxidized by the same mechanism as D-galactose
-
?
stachyose + O2
? + H2O2
-
only intracellular enzyme
-
?
stachyose + O2
? + H2O2
Polyporus circinatus
-
-
-
?
stachyose + O2
? + H2O2
Polyporus circinatus
-
best substrate tested
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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16 - 56
1-methyl-alpha-D-galactopyranoside
77 - 440
1-O-methyl-alpha-D-galactopyranoside
29 - 57
2-methylene-1,3-propanediol
0.0021 - 2950
D-galactose
0.074 - 0.16
galactoglucomannan
0.07 - 0.14
galactoxyloglucan
-
0.037 - 0.22
guar galactomannan
-
0.008 - 0.19
locust bean galactomannan
-
additional information
additional information
-
steady-state kinetics, isotope kinetics, kinetic analysis
-
16
1-methyl-alpha-D-galactopyranoside
-
mutant C383S, pH 7.0, 25°C
17
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/V494A, pH 7.0, 25°C
17
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436H, pH 7.0, 25°C
18
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436H/V494A, pH 7.0, 25°C
25
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436A, pH 7.0, 25°C
45
1-methyl-alpha-D-galactopyranoside
-
mutant Y436H/v494A, pH 7.0, 25°C
46
1-methyl-alpha-D-galactopyranoside
-
mutant V494A, pH 7.0, 25°C
46
1-methyl-alpha-D-galactopyranoside
-
mutant Y436A, pH 7.0, 25°C
46
1-methyl-alpha-D-galactopyranoside
-
mutant Y436A/V494A, pH 7.0, 25°C
47
1-methyl-alpha-D-galactopyranoside
-
mutant C383A, pH 7.0, 25°C
55
1-methyl-alpha-D-galactopyranoside
-
mutant Y436H, pH 7.0, 25°C
56
1-methyl-alpha-D-galactopyranoside
-
wild type, pH 7.0, 25°C
77
1-O-methyl-alpha-D-galactopyranoside
-
substrate oxygen at saturated 1-O-methyl-alpha-D-galactopyranoside concentration, 2 H-atoms in position 6 are substituted by D-atoms
140
1-O-methyl-alpha-D-galactopyranoside
-
substrate 1-O-methyl-alpha-D-galactopyranoside at saturated O2 concentration
190
1-O-methyl-alpha-D-galactopyranoside
-
substrate 1-O-methyl-alpha-D-galactopyranoside at saturated O2 concentration, 2 H-atoms in position 6 are substituted by D-atoms
440
1-O-methyl-alpha-D-galactopyranoside
-
substrate oxygen at saturated 1-O-methyl-alpha-D-galactopyranoside concentration
29
2-methylene-1,3-propanediol
25°C, pH 7.0, mutant enzyme W290F
57
2-methylene-1,3-propanediol
25°C, pH 7.0, wild-type enzyme
0.0021
D-galactose
-
pH 7.0, 25°C, mutant C383E
0.0084
D-galactose
-
pH 7.0, 25°C, mutant C383D
0.03
D-galactose
-
pH 7.0, 25°C, mutant C383H
0.033
D-galactose
-
pH 7.0, 25°C, mutant C383M
0.034
D-galactose
-
pH 7.0, 25°C, mutant C383S
0.048
D-galactose
-
pH 7.0, 25°C, mutant C383K
0.054
D-galactose
-
pH 7.0, 25°C, wild-type enzyme
0.055
D-galactose
-
pH 7.0, 25°C, mutant C383L
0.06
D-galactose
-
pH 7.0, 25°C, mutant C383W
0.064
D-galactose
-
pH 7.0, 25°C, mutant C383Q
0.083
D-galactose
-
pH 7.0, 25°C, mutant C383G
0.13
D-galactose
-
pH 7.0, 25°C, mutant C383F
0.14
D-galactose
-
pH 7.0, 25°C, mutant C383P
0.16
D-galactose
-
pH 7.0, 25°C, mutant C383A
0.29
D-galactose
-
pH 7.0, 25°C, mutant C383R
0.39
D-galactose
-
pH 7.0, 25°C, mutant C383N
0.43
D-galactose
-
pH 7.0, 25°C, mutant C383V
0.51
D-galactose
-
pH 7.0, 25°C, mutant C383I
0.53
D-galactose
-
pH 7.0, 25°C, mutant C383T
15
D-galactose
-
mutant C383S, pH 7.0, 25°C
16
D-galactose
-
mutant C383S/V494A, pH 7.0, 25°C
17
D-galactose
-
mutant C383S/Y436A, pH 7.0, 25°C
19
D-galactose
-
mutant C383S/Y436H/V494A, pH 7.0, 25°C
22
D-galactose
-
mutant C383S/Y436H, pH 7.0, 25°C
30
D-galactose
-
mutant Y436A/V494A, pH 7.0, 25°C
42.4
D-galactose
pH 7.0, 30°C, recombinant wild-type enzyme
45
D-galactose
25°C, pH 7.0, mutant enzyme W290H
47
D-galactose
pH 7.0, 40°C
53
D-galactose
-
mutant V494A, pH 7.0, 25°C
53
D-galactose
-
mutant Y436H, pH 7.0, 25°C
56
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant CBM29-GaO
60.4
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant GaO-CBM29
61
D-galactose
-
mutant Y436A, pH 7.0, 25°C
62
D-galactose
-
mutant C383A, pH 7.0, 25°C
68
D-galactose
-
mutant Y436H/v494A, pH 7.0, 25°C
68
D-galactose
-
wild type, pH 7.0, 25°C
82
D-galactose
25°C, pH 7.0, wild-type enzyme
132.6
D-galactose
pH 7, 30°C
1686
D-galactose
25°C, pH 7.0, mutant enzyme W290G
2950
D-galactose
25°C, pH 7.0, mutant enzyme W290F
0.074
galactoglucomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
0.13
galactoglucomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
0.16
galactoglucomannan
pH 7.0, 25°C, recombinant wild-type enzyme
0.07
galactoxyloglucan
pH 7.0, 25°C, recombinant wild-type enzyme
-
0.076
galactoxyloglucan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
0.14
galactoxyloglucan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
0.037
guar galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
0.081
guar galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
0.22
guar galactomannan
pH 7.0, 25°C, recombinant wild-type enzyme
-
0.008
locust bean galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
0.084
locust bean galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
0.19
locust bean galactomannan
pH 7.0, 25°C, recombinant wild-type enzyme
-
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457 - 1548
1-methyl-alpha-D-galactopyranoside
325
1-O-methyl beta-D-galactopyranoside
-
Cu(II)-bound H2O is required in the protonated aquo state for catalysis and is responsible for the kinetic solvent isotope effect
20 - 1165
1-O-methyl-alpha-D-galactopyranoside
1440
1-O-methyl-beta-D-galactopyranoside
-
-
166 - 283
2-methylene-1,3-propanediol
0.011 - 12243
D-galactose
3.25 - 3.98
galactoglucomannan
3.65 - 4.57
galactoxyloglucan
-
5.18 - 6.7
guar galactomannan
-
3.37 - 4.3
locust bean galactomannan
-
457
1-methyl-alpha-D-galactopyranoside
-
mutant C383A, pH 7.0, 25°C
811
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436A, pH 7.0, 25°C
839
1-methyl-alpha-D-galactopyranoside
-
mutant C383S, pH 7.0, 25°C
851
1-methyl-alpha-D-galactopyranoside
-
mutant Y436H/v494A, pH 7.0, 25°C
995
1-methyl-alpha-D-galactopyranoside
-
wild type, pH 7.0, 25°C
1039
1-methyl-alpha-D-galactopyranoside
-
mutant Y436A, pH 7.0, 25°C
1067
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436H/V494A, pH 7.0, 25°C
1091
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436H, pH 7.0, 25°C
1267
1-methyl-alpha-D-galactopyranoside
-
mutant Y436H, pH 7.0, 25°C
1444
1-methyl-alpha-D-galactopyranoside
-
mutant V494A, pH 7.0, 25°C
1495
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/V494A, pH 7.0, 25°C
1548
1-methyl-alpha-D-galactopyranoside
-
mutant Y436A/V494A, pH 7.0, 25°C
20
1-O-methyl-alpha-D-galactopyranoside
-
-
49
1-O-methyl-alpha-D-galactopyranoside
-
substrate 1-O-methyl-alpha-D-galactopyranoside, 2 H-atoms in position 6 are substituted by D-atoms
1165
1-O-methyl-alpha-D-galactopyranoside
-
substrate 1-O-methyl-alpha-D-galactopyranoside
166
2-methylene-1,3-propanediol
25°C, pH 7.0, mutant enzyme W290F
283
2-methylene-1,3-propanediol
25°C, pH 7.0, wild-type enzyme
0.011
D-galactose
-
pH 7.0, 25°C, mutant C383W
0.24
D-galactose
25°C, pH 7.0, mutant enzyme W290H
0.795
D-galactose
-
mutant C228G
1.66
D-galactose
25°C, pH 7.0, mutant enzyme W290G
2.45
D-galactose
-
mutant W290H
2.98
D-galactose
-
native wild-type enzyme
3.42
D-galactose
-
recombinant wild-type enzyme
8.8
D-galactose
-
pH 7.0, 25°C, mutant C383R
170
D-galactose
-
pH 7.0, 25°C, mutant C383Q
190
D-galactose
-
pH 7.0, 25°C, mutant C383F
210
D-galactose
-
pH 7.0, 25°C, mutant C383H
260
D-galactose
-
pH 7.0, 25°C, mutant C383I
360
D-galactose
-
pH 7.0, 25°C, mutant C383V
371
D-galactose
25°C, pH 7.0, mutant enzyme W290F
400
D-galactose
pH 7.0, 30°C, recombinant wild-type enzyme
410
D-galactose
-
pH 7.0, 25°C, mutant C383N
440
D-galactose
-
pH 7.0, 25°C, mutant C383D
450
D-galactose
-
pH 7.0, 25°C, mutant C383L
490
D-galactose
-
pH 7.0, 25°C, mutant C383P
503
D-galactose
25°C, pH 7.0, wild-type enzyme
510
D-galactose
-
pH 7.0, 25°C, mutant C383M
516.7
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant CBM29-GaO
550
D-galactose
-
pH 7.0, 25°C, mutant C383E
600
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant GaO-CBM29
639
D-galactose
-
mutant C383A, pH 7.0, 25°C
756
D-galactose
-
mutant Y436H, pH 7.0, 25°C
834
D-galactose
-
mutant C383S, pH 7.0, 25°C
915
D-galactose
-
mutant C383S/V494A, pH 7.0, 25°C
1090
D-galactose
-
wild type, pH 7.0, 25°C
1100
D-galactose
-
pH 7.0, 25°C, wild-type enzyme
1100
D-galactose
-
mutant Y436A, pH 7.0, 25°C
1100
D-galactose
-
pH 7.0, 25°C, mutant C383G
1100
D-galactose
-
pH 7.0, 25°C, mutant C383K
1100
D-galactose
-
pH 7.0, 25°C, mutant C383S
1119
D-galactose
-
mutant V494A, pH 7.0, 25°C
1181
D-galactose
-
mutant Y436H/v494A, pH 7.0, 25°C
1200
D-galactose
-
pH 7.0, 25°C, mutant C383A
1266
D-galactose
-
mutant C383S/Y436A, pH 7.0, 25°C
1301
D-galactose
-
mutant C383S/Y436H/V494A, pH 7.0, 25°C
1398
D-galactose
-
mutant Y436A/V494A, pH 7.0, 25°C
1871
D-galactose
-
mutant C383S/Y436H, pH 7.0, 25°C
3400
D-galactose
-
pH 7.0, 25°C, mutant C383T
12243
D-galactose
pH 7, 30°C
3.25
galactoglucomannan
pH 7.0, 25°C, recombinant wild-type enzyme
3.33
galactoglucomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
3.98
galactoglucomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
3.65
galactoxyloglucan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
3.68
galactoxyloglucan
pH 7.0, 25°C, recombinant wild-type enzyme
-
4.57
galactoxyloglucan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
13.7
guar
-
mutant C383A, pH 7.0, 25°C
-
26.3
guar
-
mutant Y436A, pH 7.0, 25°C
-
26.3
guar
-
mutant Y436H/v494A, pH 7.0, 25°C
-
29.7
guar
-
mutant Y436A/V494A, pH 7.0, 25°C
-
30.4
guar
-
mutant Y436H, pH 7.0, 25°C
-
32
guar
-
mutant V494A, pH 7.0, 25°C
-
37.7
guar
-
mutant C383S/Y436H, pH 7.0, 25°C
-
41.1
guar
-
mutant C383S, pH 7.0, 25°C
-
41.1
guar
-
mutant C383S/Y436A, pH 7.0, 25°C
-
42.8
guar
-
wild type, pH 7.0, 25°C
-
44.5
guar
-
mutant C383S/Y436H/V494A, pH 7.0, 25°C
-
58
guar
-
mutant C383S/V494A, pH 7.0, 25°C
-
5.18
guar galactomannan
pH 7.0, 25°C, recombinant wild-type enzyme
-
5.22
guar galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
6.7
guar galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
3.37
locust bean galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
3.57
locust bean galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
4.3
locust bean galactomannan
pH 7.0, 25°C, recombinant wild-type enzyme
-
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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
evolution
galactose oxidase is a member of the radical copper oxidase family and is classified as a member of the carbohydrate active-enzyme family AA5, subfamiliy 2
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
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
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
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
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
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
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
evolution
the enzyme belongs to the the galactose 6-oxidase/glyoxal oxidase family of mononuclear copper-radical oxidases, auxiliary activity family 5, AA5, subfamily 2, AA5_2. Structure-function analysis and comparison to other structurally related but catalytically inactive members of the family, from Colletotrichum graminicola and Colletotrichum gloeosporioides, CgrAlcOx and CglAlcOx, reveals catalytic diversity in the galactose oxidase and glyoxal oxidase family, overview. All AA5 sequences known to date contain the key active site residues of FgrGalOx, namely, C228 and Y272
evolution
-
galactose oxidase is a member of the radical copper oxidase family and is classified as a member of the carbohydrate active-enzyme family AA5, subfamiliy 2
-
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
-
metabolism
-
copper-containing complexes, namely (benzoato-kappa2O,O')[(E)-2-({[2-(diethylamino)ethyl]imino}methyl)phenolato-kappa3N,N',O]copper(II) dihydrate, [Cu(C7H5O2)(C13H19N2O)] 2H2O, [(E)-2-({[2-(diethylamino)-ethyl]imino}methyl)phenolato-kappa3N,N',O](2-phenylacetato-kappa2O,O')copper(II), [Cu-(C8H7O2)(C13H19N2O)], and bis[my-(E)-2-({[3-(diethylamino)propyl]imino}-methyl)phenolato]-kappa4N,N',O:O;kappa4O:N,N',O-(my-2-methylbenzoato-kappa2O:O')copper(II) perchlorate, [Cu2(C8H7O2)(C12H17N2O)2]ClO4, have been tested for their activity in the oxidation of D-galactose. The results suggest that, unlike the enzyme galactose oxidase, due to the precipitation of Cu2O, this reaction is not catalytic
metabolism
-
the indole ring, as an electron donor, stabilizes the phenoxyl radical by the pi-pi stacking interaction. A CuII complex of a methoxy-substituted salen-type ligand, containing a pendent indole ring on the dinitrogen chelate backbone exhibits the pi-pi stacking interaction of the indole ring mainly with one of the two phenolate moieties. The phenolate moiety in close contact with the indole moiety shows the characteristic phenoxyl radical structural features, indicating that the indole ring favors the pi-pi stacking interaction with the phenoxyl radical
physiological function
-
galactose oxidase catalyzes the 2e- oxidation of primary alcohols to aldehydes and the enzyme may also be capable of the subsequent slower 2e- oxidation to carboxylic acids. Each of these reactions is coupled to the 2e- reduction of O2 to H2O2. The native substrate of the enzyme is D-galactose, but a broad range of other sugar and aromatic alcohol substrates are also active, which has led to the proposal that the physiological role of GO is the generation of H2O2, perhaps as a defense against pathogenic organisms
physiological function
RUBY is required for the Gal oxidase activity of intact seeds, the oxidation of Gal in side-chains of rhamnogalacturonan-I present in mucilage-modified2 mucilage, but not in wild-type mucilage, the retention of branched rhamnogalacturonan-I in the seed following extrusion, and the enhancement of cell-to-cell adhesion in the seed coat epidermis
additional information
-
the catalytically relevant, oxidized state of the active site of galactose oxidase is composed of antiferromagnetically coupled Cu(II) and a posttranslationally generated Tyr-Cys radical cofactor. The thioether bond of the Tyr-Cys cross-link affects the stability, the reduction potential, and the catalytic efficiency of the enzyme active site. Electronic and geometric structures of the metal center and the coordinated [Y·-C] cofactor, computational modeling, overview. Significant difference in the spin density distribution of an isolated Tyr-Cys unit relative to its protein embedded form
additional information
-
the structure of galactose oxidase must make its catalytic activity unusually robust, permitting the enzymatic properties to survive in molecules following cleavage of the polymer chain
additional information
-
active site structure, analysis of crystal structure PDB ID 1GOF, overview. Molecular modeling of the pre-processed Cu(I)-galactose oxidase active site and biogenesis reaction coordinate
additional information
enzyme active site structure analysis of immobilzed enzyme, overview. In the active site region, the Cu ion is coordinated to two tyrosines (Tyr272 and Tyr495), two histidines (H496 and H581), and a solvent ligand (water), forming the inner coordination sphere (a type 2 centre). Importantly, Tyr272 is covalently bonded to Cys228 via a thioether bond and its radical form (Tyrc272) serves as a catalytic cofactor (i.e. the second redox site). Trp290 stacks over the Cys228 side chain and plays an essential role in generating Tyrc272 radicals for maintaining the enzyme catalytic cycles. Three-dimensional structure analysis
additional information
GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site
additional information
influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum
additional information
-
influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum
additional information
the key active site residues of FgrGalOx, C228 and Y272, combine to form the unique crosslinked thioether-tyrosyl cofactor, and Y495, H496 and H581 that also coordinate to the copper ion. Another key active site is tryptophan W290in FgrGalOx. The N-terminal CBM32 domain binds galactosyl residues. Structure-function analysis of wild-type and mutant enzymes, overview
additional information
-
the key active site residues of FgrGalOx, C228 and Y272, combine to form the unique crosslinked thioether-tyrosyl cofactor, and Y495, H496 and H581 that also coordinate to the copper ion. Another key active site is tryptophan W290in FgrGalOx. The N-terminal CBM32 domain binds galactosyl residues. Structure-function analysis of wild-type and mutant enzymes, overview
additional information
three-dimensional structure modeling based on the structure of GalOx from Fusarium graminearum
additional information
-
three-dimensional structure modeling based on the structure of GalOx from Fusarium graminearum
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
additional information
-
GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site
-
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
-
additional information
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three-dimensional structure modeling based on the structure of GalOx from Fusarium graminearum
-
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C383A
-
site-directed mutagenesis, the mutant shows 39% of wild-typ enzyme activity
C383D
-
site-directed mutagenesis, the mutant shows 26% of wild-typ enzyme activity
C383E
-
site-directed mutagenesis, the mutant shows 130% of wild-typ enzyme activity
C383F
-
site-directed mutagenesis, the mutant shows 8% of wild-typ enzyme activity
C383G
-
site-directed mutagenesis, the mutant shows 70% of wild-typ enzyme activity
C383H
-
site-directed mutagenesis, the mutant shows 35% of wild-typ enzyme activity
C383I
-
site-directed mutagenesis, the mutant shows 3% of wild-typ enzyme activity
C383K
-
site-directed mutagenesis, the mutant shows 115% of wild-typ enzyme activity
C383L
-
site-directed mutagenesis, the mutant shows 41% of wild-typ enzyme activity
C383M
-
site-directed mutagenesis, the mutant shows 75% of wild-typ enzyme activity
C383N
-
site-directed mutagenesis, the mutant shows 6% of wild-typ enzyme activity
C383P
-
site-directed mutagenesis, the mutant shows 18% of wild-typ enzyme activity
C383Q
-
site-directed mutagenesis, the mutant shows 13% of wild-typ enzyme activity
C383R
-
site-directed mutagenesis, the mutant shows 0.2% of wild-typ enzyme activity
C383S
-
site-directed mutagenesis, the mutant shows 160% of wild-typ enzyme activity
C383T
-
site-directed mutagenesis, the mutant shows 32% of wild-typ enzyme activity
C383V
-
site-directed mutagenesis, the mutant shows 4% of wild-typ enzyme activity
C383W
-
site-directed mutagenesis, the mutant shows 0.001% of wild-typ enzyme activity
C383Y
-
site-directed mutagenesis, the mutant cannt be isolated
G195E
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
M70V
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
N535D
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
V494A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
W290H
kcat/KM for D-galactose is 1180fold lower than wild-type value
C383/Y436H
-
decrease in Km-value, increase in kcat-value
C383A
-
slight decrease in Km-value, decrease in kcat-value
C383H/V494A
-
decrease in Km-value, decrease in kcat-value
C383S
-
decrease in Km-value
C383S/Y436A
-
decrease in Km-value, decrease in kcat-value of 1-methyl-alpha-D-galactose, increase in kcat-value of D-galactose
C383S/Y436H/V494A
-
decrease in Km-value, increase in kcat-value
P463I
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
P463V
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
R330K
-
the mutant shows increased activity with D-fructose compared to the wild-type enzyme
R330K/W290F/Q406E/Y405F
-
the mutant shows 136fold increased activity with D-fructose, and increased activity with mannose and N-acetylglucosamine compared to the wild-type enzyme
S10P/M70 V/P136/G195E/V494A/N535D
-
random mutagenesis, the enzyme mutant shows improved levels of recombinant expression of a more active and stable enzyme in Escherichia coli without any change in substrate range compared to the wild-type enzyme
V494A
-
slight decrease in Km-value, increase in kcat-value
W290F/R330K/Q406T
-
random mutagenesis, the mutant shows improved activity toward Glc compared to the wild-type enzyme
W290H
-
the mutant is highly activates by phosphate
Y405F/Q406E
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
Y405F/Q406Y
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
Y436A
-
Km- and kcat-values similar to wild type
Y436A/V494A
-
decrease in Km-value, increase in kcat-value
Y436H
-
slight decrease in Km-value, decrease in kcat-value
Y436H/V494A
-
slight decrease in kcat-value of 1-methyl-alpha-D-galactose, slight increase in kcat-value of D-galactose
W290H
-
the mutant is highly activates by phosphate
-
C383A
-
slight decrease in Km-value, decrease in kcat-value
-
C383S
-
decrease in Km-value
-
V494A
-
slight decrease in Km-value, increase in kcat-value
-
Y436A
-
Km- and kcat-values similar to wild type
-
Y436H
-
slight decrease in Km-value, decrease in kcat-value
-
W290H
-
analysis from X-ray structure
Y272F
-
not capable of binding copper
W290F
kcat/KM for D-galactose is 49fold lower than wild-type value, kcat/Km for 2-methylene-1,3-propanediol is 1.2fold higher than wild-type value
W290F
structure PDB ID 2EIC, comparison to the wild-type enzyme. The activity of Trp290 mutants of FgrGalOx show a dramatic loss of oxidative capacity compared to wild-type, which is correlated to significantly higher Km values for the natural substrate galactose with the FgrGalOx W290G/F mutants, presumably because of the loss of a hydrogen-bonding interaction between W290 and a remote hydroxyl group of the substrate. Trp290 in FgrGalOx is implicated in stabilizing the radical form of the Cys-Tyr cofactor, although substitution with either Phe or Gly also stabilizes the tyrosine radical with retention of catalytic activity, while other substitutions were detrimental to the enzyme
W290G
kcat/KM for D-galactose is 6370fold lower than wild-type value
W290G
the activity of Trp290 mutants of FgrGalOx show a dramatic loss of oxidative capacity compared to wild-type, which is correlated to significantly higher Km values for the natural substrate galactose with the FgrGalOx W290G/F mutants, presumably because of the loss of a hydrogen-bonding interaction between W290 and a remote hydroxyl group of the substrate. Trp290 in FgrGalOx is implicated in stabilizing the radical form of the Cys-Tyr cofactor, although substitution with either Phe or Gly also stabilizes the tyrosine radical with retention of catalytic activity, while other substitutions were detrimental to the enzyme
C228G
-
analysis from X-ray structure
C228G
-
the oxidized C228G mutant shows a higher reduction potential than the wild-type enzyme
additional information
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engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
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introduction of silent mutations within codons 2-7 of the mature enzyme coding sequence to enhance enzyme translation and have combined these with other expression-enhancing mutations
additional information
a family 29 glucomannan binding module, CBM29-1-2, from Piromyces equi is separately linked to the N- and C-termini of GaO, effects on enzyme activity and binding of GaO towards various polysaccharides. The chimeric enzyme mutants demonstrate enhanced binding to galactomannan, galactoglucomannan and galactoxyloglucan compared to the wild-type enzyme. The position of the CBM29 fusion affects the enzyme function. Particularly, C-terminal fusion leads to greatest increases in galactomannan binding and catalytic efficiency, where relative to wild-type GaO, kcat/Km values increases by 7.5 and 19.8times on guar galactomannan and locust bean galactomannan, respectively. The fusion of CBM29 also induces oligomerization of GaOCBM29. Removing CBM32 from wild-type GaO leads to complete loss in enzyme activity, and substituting the native CBM32 for CBM29-1-2 does not regain GaO function
additional information
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a family 29 glucomannan binding module, CBM29-1-2, from Piromyces equi is separately linked to the N- and C-termini of GaO, effects on enzyme activity and binding of GaO towards various polysaccharides. The chimeric enzyme mutants demonstrate enhanced binding to galactomannan, galactoglucomannan and galactoxyloglucan compared to the wild-type enzyme. The position of the CBM29 fusion affects the enzyme function. Particularly, C-terminal fusion leads to greatest increases in galactomannan binding and catalytic efficiency, where relative to wild-type GaO, kcat/Km values increases by 7.5 and 19.8times on guar galactomannan and locust bean galactomannan, respectively. The fusion of CBM29 also induces oligomerization of GaOCBM29. Removing CBM32 from wild-type GaO leads to complete loss in enzyme activity, and substituting the native CBM32 for CBM29-1-2 does not regain GaO function
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
genetic incorporation of 3,5-dichlorotyrosine (Cl2-Tyr) and 3,5-difluorotyrosine (F2-Tyr) to replace Tyr272 in the GAOV variant (i.e. A3.E7) optimized for expression through directed evolution. The proteins with an unnatural tyrosine residue are catalytically competent
additional information
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engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
identification of variants of GOase that possess good activity towards a range of secondary alcohols based upon the 1-phenylethanol template and high enantioselectivity in the kinetic resolution of (+/-)-3-fluoro-1-phenylethanol
additional information
-
glycoprotein labeling using engineered variants of galactose oxidase obtained by directed evolution, overview. The methodology can also be applied to the labeling of cells. Pichia pastoris cells, which express mannosylated glycoproteins on their surface
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
-
additional information
the enzyme is immobilized in a nanoscale chemical environment provided by mesoporous silicas (MPS). Two types of MPS, i.e. SBA-15 and MCF, are synthesized and used to accommodate GAOX. SBA-15-ROD are rod-shaped particles with periodically ordered nanopores (9.5 nm), while MCF has a mesocellular foam-like structure with randomly distributed pores (23 nm) interconnected by smaller windows (8.8 nm). GAOX is non-covalently bound to SBA-15-ROD, while it is covalently immobilized on MCF. Relatively high loadings in the range of 50-60 mg/g are achieved. The catalytic kinetics is reduced, mainly attributed to the diffusion limitation of substrate and product in the nanoscale channels. The apparent KM of the enzyme is largely unchanged upon immobilization, while the turnover number (kcat) is slightly reduced. The overall catalytic efficiency, represented by the ratio of kcat/KM, is retained around 70% and 60% for SBA-15 and MCF immobilization, respectively. The thermal resistance is enhanced up to 60°C, but with no further enhancement above 60°C. Three-dimensional structure analysis of immobilzed enzyme, overview
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Catalytic reaction profile for alcohol oxidation by galactose oxidase
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Hypomyces rosellus
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Hypomyces rosellus
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Structure and mechanism of galactose oxidase. The free radical site
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Hypomyces rosellus
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Hypomyces rosellus
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Hypomyces rosellus
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Purification of galactose oxidase from Dactylium dendroides by affinity chromatography on melibiose-polyacrylamide
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263
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1988
Hypomyces rosellus
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Bretting, H.; Jacobs, G.
The reactivity of galactose oxidase with snail galactans, galactosides and D-galactose-composed oligosaccharides
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1987
Hypomyces rosellus
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Solvent and solvent proton dependent steps in the galactose oxidase reaction
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1987
Hypomyces rosellus
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Purification and characterization of intracellular galactose oxidase from Dactylium dendroides
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252
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1987
Hypomyces rosellus
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Hypomyces rosellus
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Catalytic properties of Gibberella galactose oxidase
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Oxidation rates of some desialylated glycoproteins by galactose oxidase
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Hypomyces rosellus
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Fusarium fujikuroi
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Substrate specificity of D-galactose oxidase
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Hypomyces rosellus
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Galactose oxidase from Dactylium dendroides
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Hypomyces rosellus
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Stereospecific oxidation of aliphatic alcohols catalyzed by galactose oxidase
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1982
Hypomyces rosellus
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1982
Polyporus circinatus
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Hypomyces rosellus
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Purification and properties of galactose oxidase from Gibberella fujikuroi
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-
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Hypomyces rosellus
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1977
Hypomyces rosellus
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1976
Hypomyces rosellus
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The molecular properties of the copper enzyme galactose oxidase
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1974
Hypomyces rosellus
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Superoxide dismutase activity of galactose oxidase
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1974
Polyporus circinatus
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Trivalent copper, superoxide, and galactose oxidase
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Hypomyces rosellus, Polyporus circinatus
-
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Polyporus circinatus
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Hypomyces rosellus
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Hypomyces rosellus
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Hypomyces rosellus
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Aspergillus sp.
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Fusarium acuminatum
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Paenibacillus sp. AIU 311
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2008
Fusarium graminearum (P0CS93)
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Parikka, K.; Tenkanen, M.
Oxidation of methyl alpha-D-galactopyranoside by galactose oxidase: products formed and optimization of reaction conditions for production of aldehyde
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2009
Fusarium sp.
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2009
Hypomyces rosellus
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Humphreys, K.J.; Mirica, L.M.; Wang, Y.; Klinman, J.P.
Galactose oxidase as a model for reactivity at a copper superoxide center
J. Am. Chem. Soc.
131
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2009
Hypomyces rosellus
brenda
Rokhsana, D.; Dooley, D.; Szilagyi, R.
Systematic development of computational models for the catalytic site in galactose oxidase: Impact of outer-sphere residues on the geometric and electronic structures
J. Biol. Inorg. Chem.
13
371-383
2008
Hypomyces rosellus
brenda
Sasaki, Y.; Kataoka, M.; Urano, N.; Ogawa, J.; Iwasaki, A.; Hasegawa, J.; Isobe, K.; Shimizu, S.
Cloning, sequencing and expression analysis of a gene encoding alcohol oxidase in Paenibacillus sp. AIU 311
J. Biosci. Bioeng.
110
147-151
2010
Paenibacillus sp.
brenda
Deacon, S.E.; McPherson, M.J.
Enhanced expression and purification of fungal galactose oxidase in Escherichia coli and use for analysis of a saturation mutagenesis library
ChemBioChem
12
593-601
2011
Fusarium graminearum
brenda
Rokhsana, D.; Howells, A.E.; Dooley, D.M.; Szilagyi, R.K.
Role of the Tyr-Cys cross-link to the active site properties of galactose oxidase
Inorg. Chem.
51
3513-3524
2012
Hypomyces rosellus
brenda
Parikka, K.; Leppnen, A.; Pitknen, L.; Reunanen, M.; Willfr, S.; Tenkanen, M.
Oxidation of polysaccharides by galactose oxidase
J. Agric. Food Chem.
58
262-271
2010
Fusarium sp.
brenda
Rannes, J.B.; Ioannou, A.; Willies, S.C.; Grogan, G.; Behrens, C.; Flitsch, S.L.; Turner, N.J.
Glycoprotein labeling using engineered variants of galactose oxidase obtained by directed evolution
J. Am. Chem. Soc.
133
8436-8439
2011
Fusarium sp.
brenda
Kempner, E.; Whittaker, J.; Miller, J.
Radiation inactivation of galactose oxidase, a monomeric enzyme with a stable free radical
Protein Sci.
19
236-241
2010
Hypomyces rosellus
brenda
Mollerup, F.; Parikka, K.; Vuong, T.V.; Tenkanen, M.; Master, E.
Influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum
Biochim. Biophys. Acta
1860
354-362
2016
Fusarium graminearum (P0CS93), Fusarium graminearum
brenda
Anasontzis, G.E.; Salazar Pena, M.; Spadiut, O.; Brumer, H.; Olsson, L.
Effects of temperature and glycerol and methanol-feeding profiles on the production of recombinant galactose oxidase in Pichia pastoris
Biotechnol. Prog.
30
728-735
2014
Fusarium graminearum (P0CS93), Fusarium graminearum, Fusarium graminearum SMD1168H (P0CS93)
brenda
Cowley, R.E.; Cirera, J.; Qayyum, M.F.; Rokhsana, D.; Hedman, B.; Hodgson, K.O.; Dooley, D.M.; Solomon, E.I.
Structure of the reduced copper active site in preprocessed galactose oxidase ligand tuning for one-electron O2 activation in cofactor biogenesis
J. Am. Chem. Soc.
138
13219-13229
2016
Hypomyces rosellus
brenda
Parikka, K.; Master, E.; Tenkanen, M.
Oxidation with galactose oxidase multifunctional enzymatic catalysis
J. Mol. Catal. B
120
47-59
2015
Fusarium acuminatum, Fusarium subglutinans, Fusarium subglutinans (A0A0U1YLU5), Fusarium konzum, Fusarium thapsinum, Fusarium nygamai, Fusarium verticillioides (E6PBN6), Fusarium graminearum (P0CS93), Fusarium verticillioides 7600 (E6PBN6)
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brenda
Yin, D.T.; Urresti, S.; Lafond, M.; Johnston, E.M.; Derikvand, F.; Ciano, L.; Berrin, J.G.; Henrissat, B.; Walton, P.H.; Davies, G.J.; Brumer, H.
Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family
Nat. Commun.
6
10197
2015
Fusarium graminearum (P0CS93), Fusarium graminearum
brenda
Toftgaard Pedersen, A.; Birmingham, W.; Rehn, G.; Charnock, S.; Turner, N.; Woodley, J.
Process requirements of galactose oxidase catalyzed oxidation of alcohols
Org. Process Res. Dev.
19
1580-1589
2015
Fusarium sp., Fusarium sp. NRLL 2903
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brenda
Paukner, R.; Staudigl, P.; Choosri, W.; Sygmund, C.; Halada, P.; Haltrich, D.; Leitner, C.
Galactose oxidase from Fusarium oxysporum - expression in E. coli and P. pastoris and biochemical characterization
PLoS ONE
9
e100116
2014
Fusarium oxysporum (V5NQ89), Fusarium oxysporum G12 (V5NQ89), Fusarium oxysporum G12
brenda
Paukner, R.; Staudigl, P.; Choosri, W.; Haltrich, D.; Leitner, C.
Expression, purification, and characterization of galactose oxidase of Fusarium sambucinum in E. coli
Protein Expr. Purif.
108
73-79
2015
Fusarium sambucinum (A0A089QAB6), Fusarium sambucinum, Fusarium sambucinum MA1886 (A0A089QAB6)
brenda
Ikemoto, H.; Mossin, S.; Ulstrup, J.; Chi, Q.
Probing structural and catalytic characteristics of galactose oxidase confined in nanoscale chemical environments
RSC Adv.
4
21939-21950
2014
Hypomyces rosellus (P0CS93)
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brenda
Mattey, A.; Birmingham, W.; Both, P.; Kress, N.; Huang, K.; Van Munster, J.; Bulmer, G.; Parmeggiani, F.; Voglmeir, J.; Martinez, J.; Turner, N.; Flitsch, S.
Selective oxidation of N-glycolylneuraminic acid using an engineered galactose oxidase variant
ACS Catal.
9
8208-8212
2019
Fusarium graminearum (P0CS93)
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brenda
Dimeska, R.; Wikaira, J.; Mockler, G.; Butcher, R.
The crystal and molecular structures of three copper-containing complexes and their activities in mimicking galactose oxidase
Acta Crystallogr. Sect. C
75
538-544
2019
synthetic construct
brenda
Oshita, H.; Suzuki, T.; Kawashima, K.; Abe, H.; Tani, F.; Mori, S.; Yajima, T.; Shimazaki, Y.
Pi-pi stacking interaction in an oxidized CuII -salen complex with a side-chain indole ring an approach to the function of the tryptophan in the active site of galactose oxidase
Chemistry
25
7649-7658
2019
synthetic construct
brenda
Li, J.; Davis, I.; Griffith, W.P.; Liu, A.
Formation of monofluorinated radical cofactor in galactose oxidase through copper-mediated C-F bond scission
J. Am. Chem. Soc.
142
18753-18757
2020
Fusarium graminearum (P0CS93)
brenda
Yin, Z.; Zhi, J.
A photoelectrochemical biosensor based on the direct electron transfer to galactose oxidase
J. Photochem. Photobiol. A
397
112560
2020
Hypomyces rosellus
-
brenda
Faria, C.B.; de Castro, F.F.; Martim, D.B.; Abe, C.A.L.; Prates, K.V.; de Oliveira, M.A.S.; Barbosa-Tessmann, I.P.
Production of galactose oxidase inside the Fusarium fujikuroi species complex and recombinant expression and characterization of the galactose oxidase GaoA protein from Fusarium subglutinans
Mol. Biotechnol.
61
633-649
2019
Fusarium subglutinans (A0A0U1YLU5), Fusarium subglutinans
brenda
Johnson, H.C.; Zhang, S.; Fryszkowska, A.; Ruccolo, S.; Robaire, S.A.; Klapars, A.; Patel, N.R.; Whittaker, A.M.; Huffman, M.A.; Strotman, N.A.
Biocatalytic oxidation of alcohols using galactose oxidase and a manganese(III) activator for the synthesis of islatravir
Org. Biomol. Chem.
19
1620-1625
2021
Fusarium graminearum (P0CS93)
brenda
Sola, K.; Gilchrist, E.J.; Ropartz, D.; Wang, L.; Feussner, I.; Mansfield, S.D.; Ralet, M.C.; Haughn, G.W.
RUBY, a putative galactose oxidase, influences pectin properties and promotes cell-to-cell adhesion in the seed coat epidermis of Arabidopsis
Plant Cell
31
809-831
2019
Arabidopsis thaliana (Q93Z02)
brenda
Sola, K.; Dean, G.H.; Li, Y.; Lohmann, J.; Movahedan, M.; Gilchrist, E.J.; Adams, K.L.; Haughn, G.W.
Expression patterns and functional characterisation of Arabidopsis galactose oxidase-like genes suggest specialised roles for galactose oxidases in plants
Plant Cell Physiol.
62
1927-1943
2021
Arabidopsis thaliana (F4K172), Arabidopsis thaliana (Q9FYG4), Arabidopsis thaliana (Q9LR03), Arabidopsis thaliana (Q9M332), Arabidopsis thaliana (Q9M9S1), Arabidopsis thaliana (Q9SVX6)
brenda