1.1.3.9: galactose oxidase
This is an abbreviated version!
For detailed information about galactose oxidase, go to the full flat file.
Word Map on EC 1.1.3.9
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1.1.3.9
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neuraminidase
-
copper
-
borohydride
-
lymphocyte
-
lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
-
glycolipids
-
galactosyl
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glycoconjugates
-
agglutinin
-
nab3h4
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ganglioside
-
dendroides
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phenoxyl
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hydrazide
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sialylation
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borotritide
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graminearum
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one-electron
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sialoglycoproteins
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sialidase
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galactosamine
-
copper-containing
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n-acetylgalactosaminyl
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desialylated
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naio4
-
synthesis
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lactoperoxidase
-
galactose-containing
-
degradation
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diagnostics
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molecular biology
-
energy production
-
analysis
-
biotechnology
- 1.1.3.9
- neuraminidase
- copper
- borohydride
- lymphocyte
- lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
- glycolipids
-
galactosyl
- glycoconjugates
- agglutinin
-
nab3h4
- ganglioside
- dendroides
-
phenoxyl
- hydrazide
-
sialylation
-
borotritide
- graminearum
-
one-electron
-
sialoglycoproteins
- sialidase
- galactosamine
-
copper-containing
-
n-acetylgalactosaminyl
-
desialylated
- naio4
- synthesis
- lactoperoxidase
-
galactose-containing
- degradation
- diagnostics
- molecular biology
- energy production
- analysis
- biotechnology
Reaction
Synonyms
AOd, At1g14430, At1g19900, At1g67290, At1g75620, At3g53950, At3g57620, At5g19580, beta-galactose oxidase, D-galactose oxidase, F5K20_250, FgrGalOx, galactose 6-oxidase, galactose oxidase, GalOx, GAO, GAOA, GAOX, GLOX1, Glox2, Glox3, GLOX4, GLOX5, GLOX6, GO, GOase, RUBY, RUBY PARTICLES IN MUCILAGE
ECTree
1.1.3.9 galactose oxidaseAdvanced search results
results (
results (Natural Substrates Products
Natural Substrates Products on EC 1.1.3.9 - galactose oxidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-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
-
-
-
?
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-glucosylpyranoside + O2
D-gluco-hexodialdose + H2O2
-
very low activity
-
?
Forssman glycolipid + O2
? + H2O2
-
higher activity as vesicle-bound substrate, very low activity as free substrate
-
?
Gal-beta-(1-3)-[Fuc-alpha-(1-2)]-GalNAcol + O2
? + H2O2
-
no oxidation of oligosaccharides containing N-acetylgalactosamine at the non-reducing end
-
?
globoside + O2
? + H2O2
-
human and porcine globoside, vesicle-bound and free substrate, best substrate tested
-
?
mucin + O2
? + H2O2
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bovine submaxillary mucin, native and desialylated
-
?
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
-
-
-
?
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
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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
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i.e. D-cellobiose
-
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
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67% of the activity compared to D-galactose
-
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
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low activity
-
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
low activity
-
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
high activity
-
?
D-galactosamine + O2
? + H2O2
-
46% of the activity compared to D-galactose
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
two binding sites for D-galactose, highly specific for O2 as electron acceptor
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
high degree of hexose specificity
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
-
-
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
shows also superoxide dismutase activity
-
?
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
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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
-
?
raffinose + O2
? + H2O2
-
more rapidly oxidized than D-galactose
-
?
raffinose + O2
? + H2O2
Polyporus circinatus
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more rapidly oxidized than D-galactose
-
?
stachyose + O2
? + H2O2
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oligosaccharides containing D-galactose at the nonreducing end are oxidized by the same mechanism as D-galactose
-
?
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
-
-
?
