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Information on EC 1.1.3.9 - galactose oxidase
for references in articles please use BRENDA:EC1.1.3.9
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.9 galactose oxidase
IUBMB Comments
A copper protein.
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
galactose oxidase, goase, d-galactose oxidase, galactose 6-oxidase, galox, ruby particles in mucilage, fgrgalox, glox2, glox1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-galactose oxidase
-
-
-
-
D-galactose oxidase
-
-
-
-
galactose 6-oxidase
galactose oxidase
GalOx
GAO
GAOA
GAOX
GO
GOase
GAO
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-galactose + O2 = D-galacto-hexodialdose + H2O2
-
-
-
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
detailed mechanism, selective for pro-S hydrogen abstraction
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
the active site consists of two one-electron redox units involving residues Y495, H496, H581, Y272, and W290, a Cu2+ ion, and a crosslinked Y272-C228 radical cofactor, which together are responsible for the catalytic activity, structure modelling
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
reaction mechanism, structure-function analysis, two-electron redox reaction involving a Cu(I)/Cu(II) couple and the reversible oxidation of a ligating phenolate, tyrosine residue of the Tyr272-Cys228 conjugate, to a phenoxyl radical, overview
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
detailed reaction mechanism, the active site of galactose oxidase bears a Cu2+ with an inner coordination sphere involving Tyr272, Tyr495, His496, His581, and a coordinated solvent molecule, and Trp290 in the outer sphere of the complex, overview
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
the first half-reaction involves proton transfer from O-6 of galactose to the axial tyrosine anion, hydrogen atom transfer (HAT) from C-6 of galactose to the tyrosine-cysteine radical cofactor and electron transfer from the carbohydrate to generate the aldehyde and Cu(I). To complete the catalytic cycle, the second half-reaction is proposed to involve inner-sphere electron transfer from Cu(I) to oxygen to yield superoxide, HAT from the phenolic hydroxyl group of the Tyr-Cys cofactor to the superoxide to produce metal-bound hydroperoxide and proton transfer from the axial tyrosine to hydroperoxide to produce hydrogen peroxide and the re-oxidized, active Cu(II)-radical state of the enzyme
D-galactose + O2 = D-galacto-hexodialdose + H2O2
the catalytic mechanism of enzyme GOase can be described by the ping-pong bi bi mechanism, where the alcohol substrate is oxidized in one catalytic halfreaction followed by reoxidation of the enzyme by reduction of oxygen to hydrogen peroxide in a second half-reaction
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
D-galactose + O2 = D-galacto-hexodialdose + H2O2
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde
-
-
D-galactose + O2 = D-galacto-hexodialdose + H2O2
the catalytic mechanism of enzyme GOase can be described by the ping-pong bi bi mechanism, where the alcohol substrate is oxidized in one catalytic halfreaction followed by reoxidation of the enzyme by reduction of oxygen to hydrogen peroxide in a second half-reaction
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
D-galactose:oxygen 6-oxidoreductase
A copper protein.
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CAS REGISTRY NUMBER
COMMENTARY
9028-79-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(furan-2-yl)methanol + O2
furan-2-carbaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
1-methyl-alpha-D-galactopyranoside + O2
? + H2O2
Substrates: 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
Products: -
Products: -
?
1-O-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
1-O-methyl-D-galactopyranoside + O2
?
-
Substrates: 112% of the activity with D-galactose
Products: -
Products: -
?
2-ethynylglycerol + O2
(2R)-2-ethynylglyceraldehyde + H2O2
Substrates: -
Products: -
Products: -
?
2-glycerol-alpha-D-galactosylpyranoside + O2
2-glycerol-alpha-D-galactosyl-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: low activity
Products: -
Products: -
?
3-bromo-1,2-propanediol + O2
? + H2O2
-
Substrates: -
Products: S isomer
Products: S isomer
?
3-bromobenzyl alcohol + O2
3-bromobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-chloro-1,2-propanediol + O2
? + H2O2
-
Substrates: only R isomer will have the correct orientation to react with the enzyme
Products: S isomer
Products: S isomer
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzyl alcohol + O2
3-nitrobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-(methylthio)benzyl alcohol + O2
4-(methylthio)benzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-(trifluoromethyl)benzyl alcohol + O2
4-(trifluoromethyl)benzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-bromobenzyl alcohol + O2
4-bromobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-fluorobenzyl alcohol + O2
4-fluorobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-iodobenzyl alcohol + O2
4-iodobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-methylbenzyl alcohol + O2
4-methylbenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzyl alcohol + O2
4-nitrobenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
allyl alcohol + O2
acrolein + H2O2
-
Substrates: only extracelluar enzyme, low activity
Products: -
Products: -
?
benzene-1,2-diamine + O2
? + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
benzylalcohol + O2
benzaldehyde + H2O2
-
Substrates: substrate reaction profiling
Products: -
Products: -
?
beta-D-galactopyranosyl-(1-6)-beta-D-galactopyranosyl-(1-4)-D-glucose + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
beta-D-galactosyl-(1-6)-beta-D-galactopyranoside + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
beta-hydroxypyruvate + O2
2,3-dioxopropionate + H2O2
-
Substrates: only extracellular enzyme, low activity
Products: -
Products: -
?
beta-thiogalactoside + O2
beta-thiogalacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: more rapidly oxidized than beta-D-galactose
Products: -
Products: -
?
ceramide dihexoside + O2
? + H2O2
-
Substrates: higher activity than free substrate, very low activity as vesicle-bound substrate
Products: -
Products: -
?
ceramide trihexoside + O2
? + H2O2
-
Substrates: vesicle-bound and free substrate
Products: -
Products: -
?
D-Gal-beta-(1-3)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
Substrates: low activity
Products: -
Products: -
?
D-Gal-beta-(1-3)-D-Gal-beta-(1-3)-D-Gal-(1-1)-L-Gro + O2
? + H2O2
-
Substrates: low activity
Products: -
Products: -
?
D-Gal-beta-(1-3)-D-Gal-beta-(1-6)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
Substrates: lower activity than with a reversed beta-1-6-linkage
Products: -
Products: -
?
D-Gal-beta-(1-3)-[D-Gal-beta-(1-6)]-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
Substrates: best oligosaccharide oxidized
Products: -
Products: -
?
D-Gal-beta-(1-6)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
Substrates: faster oxidation than corresponding beta-1-3-linked components
Products: -
Products: -
?
D-Gal-beta-(1-6)-D-Gal-beta-(1-3)-D-Gal-beta-(1-1)-L-Gro + O2
? + H2O2
-
Substrates: improved activity
Products: -
Products: -
?
D-galactopyranose + ferricyanide
D-galacto-hexodialdose + ferrocyanide
-
Substrates: ferricyanide poorly replaces O2 as electron acceptor
Products: -
Products: -
?
D-glucosylpyranoside + O2
D-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
fetuin + O2
? + H2O2
-
Substrates: bovine fetuin, native or desialylated
Products: -
Products: -
?
Forssman glycolipid + O2
? + H2O2
-
Substrates: higher activity as vesicle-bound substrate, very low activity as free substrate
Products: -
Products: -
?
Gal-beta-(1-3)-[Fuc-alpha-(1-2)]-GalNAcol + O2
? + H2O2
-
Substrates: no oxidation of oligosaccharides containing N-acetylgalactosamine at the non-reducing end
Products: -
Products: -
?
galactan + O2
? + H2O2
-
Substrates: derived from snail, Lymnea stagnalis galactan best substrate
Products: -
Products: -
?
galactogen + O2
? + H2O2
-
Substrates: substrate from Helix pomatia, galactose oxidase acts upon a specific subterminal nonreducing D-galactosyl residue
Products: -
Products: -
?
galactose 1-phosphate + O2
? + H2O2
Polyporus circinatus
-
Substrates: very low activity
Products: -
Products: -
?
galactose-4-SO3Na + O2
? + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
galactose-6-SO3Na + O2
? + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
globoside + O2
? + H2O2
-
Substrates: human and porcine globoside, vesicle-bound and free substrate, best substrate tested
Products: -
Products: -
?
glyceraldehyde + O2
? + H2O2
-
Substrates: 70% of the activity with glycolaldehyde
Products: -
Products: -
?
glycoaldehyde + O2
glyoxal + H2O2
-
Substrates: only extracellular enzyme, low activity
Products: -
Products: -
?
hexadecyl-(ethyleneglycol)13-D-galactose + O2
hexadecyl-(ethyleneglycol)13-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
hexadecyl-(ethyleneglycol)20-D-galactose + O2
hexadecyl-(ethyleneglycol)20-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
hexadecyl-(ethyleneglycol)6-D-galactose + O2
hexadecyl-(ethyleneglycol)6-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
hexadecyl-(ethyleneglycol)9-D-galactose + O2
hexadecyl-(ethyleneglycol)9-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
isopropyl-beta-D-thiogalactosylpyranoside + O2
isopropyl-beta-D-thiogalactosyl-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: 43% of the activity compared to D-galactose
Products: -
Products: -
?
L-glucose + O2
L-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
locust bean galactomannan + O2
?
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
methyl beta-D-thiogalactosylpyranoside + O2
methyl beta-D-thiogalacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
mucin + O2
? + H2O2
-
Substrates: bovine submaxillary mucin, native and desialylated
Products: -
Products: -
?
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
Substrates: 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
Products: -
Products: -
?
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
-
Substrates: more reactive than p-nitrophenyl-beta-D-galactoside
Products: -
Products: -
?
p-nitrophenyl beta-D-galactoside + O2
1-O-(p-nitrophenyl)-beta-D-galactohexodialdose + H2O2
-
Substrates: less reactive than p-nitrophenyl-alpha-D-galactoside
Products: -
Products: -
?
1-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-methyl-alpha-D-galactopyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: best substrate
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: best substrate
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: high activity
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: high activity
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
-
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: 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
Products: -
Products: -
?
1-methyl-beta-D-galactopyranoside + O2
? + H2O2
Substrates: 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
Products: -
Products: -
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
ir
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: very fast reaction
Products: -
Products: -
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: less reactive than nitrophenyl alpha-galactosides
Products: -
Products: -
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
-
Substrates: unusually large kinetic isotope effect for oxidation of the alpha-deuterated alcohol
Products: -
Products: -
?
1-O-methyl-alpha-D-galactosylpyranoside + O2
1-O-methyl-alpha-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-alpha-D-glucosylpyranoside + O2
1-O-methyl-alpha-D-gluco-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-alpha-D-glucosylpyranoside + O2
1-O-methyl-alpha-D-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
Substrates: beta-configuration preferred
Products: -
Products: -
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
Substrates: less reactive than nitrophenyl alpha-galactosides
Products: -
Products: -
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
Substrates: 48% higher activity compared to D-galactose
Products: -
Products: -
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1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
Substrates: 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
Products: -
Products: -
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1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
-
Substrates: one or more tryptophan residues, the Cu(II) atom and the sugar substrate interact within the native enzyme
Products: -
Products: -
?
1-O-methyl-beta-D-galactosylpyranoside + O2
1-O-methyl-beta-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: highly active
Products: -
Products: -
?
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-beta-D-glucosylpyranoside + O2
1-O-methyl-beta-D-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
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2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
Substrates: -
Products: -
Products: -
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2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
Substrates: responsible for the conversion of galactosyl residues to the corresponding aldehydes and uronic acids
Products: -
Products: -
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
-
Substrates: 52% of the activity compared to D-galactose
Products: -
Products: -
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
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4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
-
Substrates: i.e. D-cellobiose
Products: -
Products: -
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alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
Substrates: 67% of the activity compared to D-galactose
Products: -
Products: -
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
Substrates: low activity
Products: -
Products: -
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beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
Substrates: high activity
Products: -
Products: -
?
D-galactosamine + O2
? + H2O2
-
Substrates: 46% of the activity compared to D-galactose
Products: -
Products: -
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: the overall catalytic reaction can be split into two half-reactions, i.e. oxidative and reductive half-reactions
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
Substrates: two binding sites for D-galactose, highly specific for O2 as electron acceptor
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
389850, 389851, 389853, 389854, 389855, 389856, 389858, 389859, 389860, 389862, 389871, 389872, 389875, 389876, 389877, 389879
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
Substrates: high degree of hexose specificity
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: shows also superoxide dismutase activity
Products: -
Products: -
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
Substrates: 150% of the activity with D-galactose
Products: -
Products: -
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
Substrates: most rapidly oxidized by the same mechanism as for D-galactose
Products: -
Products: -
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
Substrates: best substrate for both intra- and extracellular enzymes
Products: -
Products: -
?
ganglioside + O2
? + H2O2
Polyporus circinatus
-
Substrates: bovine brain gangliosides in 70% n-propanol, in aqueous solution not a substrate
Products: -
Products: -
?
ganglioside + O2
? + H2O2
Polyporus circinatus
-
Substrates: gangliosides from bovine brain as free molecules and micellar or vesicular dispersions
Products: -
Products: -
?
glycerol + O2
(S)-glyceraldehyde + H2O2
-
Substrates: only extracelluar enzyme, low activity
Products: -
Products: -
?
glycerol + O2
(S)-glyceraldehyde + H2O2
-
Substrates: enzyme exhibits prochiral specificity
Products: -
Products: -
?
glycolaldehyde + O2
glyoxal + H2O2
-
Substrates: -
Products: approximately 35 mM of glyoxal is produced from 85 mM glycolaldehyde after 7 d of incubation at 50°C and pH 5.5
Products: approximately 35 mM of glyoxal is produced from 85 mM glycolaldehyde after 7 d of incubation at 50°C and pH 5.5
?
guaran + O2
? + H2O2
-
Substrates: only intracellular enzyme
Products: -
Products: -
?
lactose + O2
?
-
Substrates: 4% of the activity with D-galactose
Products: -
Products: -
?
melibiose + O2
?
-
Substrates: 103% of the activity with D-galactose
Products: -
Products: -
?
melibiose + O2
? + H2O2
Substrates: high catalytic efficiency
Products: -
Products: -
?
melibiose + O2
? + H2O2
Substrates: high catalytic efficiency
Products: -
Products: -
?
methyl alpha-D-galactopyranoside + O2
methyl alpha-D-galacto-hexodialdo-1,5-pyranoside + H2O2
-
Substrates: 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
Products: -
Products: -
?
methyl alpha-D-galactopyranoside + O2
methyl alpha-D-galacto-hexodialdo-1,5-pyranoside + H2O2
Substrates: -
Products: -
Products: -
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-galactoside + O2
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-galactoside + O2
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
-
Substrates: ortho-isomer 3 times more potent than para- and meso-forms, 14% of the activity compared to D-galactose
Products: -
Products: -
?
o-nitrophenyl beta-D-galactoside + O2
1-O-(o-nitrophenyl)-alpha-D-galactohexodialdose + H2O2
Polyporus circinatus
-
Substrates: low activity
Products: -
Products: -
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
Substrates: -
Products: -
Products: -
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
Substrates: -
Products: -
Products: -
?
raffinose + O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
Substrates: -
Products: -
Products: -
?
raffinose + O2
?
-
Substrates: 134% of the activity with D-galactose
Products: -
Products: -
?
raffinose + O2
? + H2O2
-
Substrates: more rapidly oxidized than D-galactose
Products: -
Products: -
?
raffinose + O2
? + H2O2
-
Substrates: same activity as for D-galactose
Products: -
Products: -
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
Substrates: more rapidly oxidized than D-galactose
Products: -
Products: -
?
stachyose + O2
? + H2O2
-
Substrates: oligosaccharides containing D-galactose at the nonreducing end are oxidized by the same mechanism as D-galactose
Products: -
Products: -
?
stachyose + O2
? + H2O2
-
Substrates: only intracellular enzyme
Products: -
Products: -
?
stachyose + O2
? + H2O2
Polyporus circinatus
-
Substrates: best substrate tested
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: generation and identification of functional models for GOase based on peptide ligand libraries, combinatorial method, low-molecular-weight model systems for GOase, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, no or poor activity with lactose, D-glucose, and guar gum, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows broad primary alcohol substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: benzyl alcohol is also a substrate for the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: benzyl alcohol is also a substrate for the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: no substrate: D-glucose
Products: -
Products: -
?
additional information
?
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Substrates: no substrate: D-glucose
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: affinity of enzyme for amphiphiles with larger ethyleneglycol spacer is much larger than for free D-galactose and beta-D-galactopyranosides
Products: -
Products: -
?
additional information
?
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Substrates: more than 95% selectivity for pro-S hydrogen abstraction
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
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Substrates: the recombinant alcohol oxidase also exhibits aldehyde alcohol oxidase activity and superoxide dismutase activity
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: -
Products: -
?
beta-D-galactosyl-(1-6)-beta-D-galactopyranoside + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
ceramide dihexoside + O2
? + H2O2
-
Substrates: higher activity than free substrate, very low activity as vesicle-bound substrate
Products: -
Products: -
?
ceramide trihexoside + O2
? + H2O2
-
Substrates: vesicle-bound and free substrate
Products: -
Products: -
?
D-glucosylpyranoside + O2
D-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
fetuin + O2
? + H2O2
-
Substrates: bovine fetuin, native or desialylated
Products: -
Products: -
?
Forssman glycolipid + O2
? + H2O2
-
Substrates: higher activity as vesicle-bound substrate, very low activity as free substrate
Products: -
Products: -
?
Gal-beta-(1-3)-[Fuc-alpha-(1-2)]-GalNAcol + O2
? + H2O2
-
Substrates: no oxidation of oligosaccharides containing N-acetylgalactosamine at the non-reducing end
Products: -
Products: -
?
globoside + O2
? + H2O2
-
Substrates: human and porcine globoside, vesicle-bound and free substrate, best substrate tested
Products: -
Products: -
?
mucin + O2
? + H2O2
-
Substrates: bovine submaxillary mucin, native and desialylated
Products: -
Products: -
?
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
Substrates: -
Products: -
Products: -
?
2 raffinose + 2 O2
6''-aldehydoraffinose + 6''-carboxyraffinose + H2O2 + H2O
-
Substrates: responsible for the conversion of galactosyl residues to the corresponding aldehydes and uronic acids
Products: -
Products: -
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
-
Substrates: 52% of the activity compared to D-galactose
Products: -
Products: -
?
2-deoxy-D-galactose + O2
2-deoxy-D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
4-O-beta-D-glucopyranosyl-D-glucose + O2
4-O-beta-D-glucopyranosyl-D-gluco-hexodialdose + H2O2
-
Substrates: i.e. D-cellobiose
Products: -
Products: -
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
-
Substrates: 67% of the activity compared to D-galactose
Products: -
Products: -
?
alpha-D-talose + O2
alpha-D-talo-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
Substrates: low activity
Products: -
Products: -
?
beta-D-lactose + O2
beta-D-lacto-hexodialdose + H2O2
-
Substrates: high activity
Products: -
Products: -
?
D-galactosamine + O2
? + H2O2
-
Substrates: 46% of the activity compared to D-galactose
Products: -
Products: -
?
D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactose + O2
D-galacto-hexodialdose + H2O2
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
Substrates: two binding sites for D-galactose, highly specific for O2 as electron acceptor
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
389850, 389851, 389853, 389854, 389855, 389856, 389858, 389859, 389860, 389862, 389871, 389872, 389875, 389876, 389877, 389879
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
-
Substrates: high degree of hexose specificity
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
D-galactosylpyranoside + O2
D-galacto-hexodialdose + H2O2
Polyporus circinatus
-
Substrates: shows also superoxide dismutase activity
Products: -
Products: -
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
Substrates: most rapidly oxidized by the same mechanism as for D-galactose
Products: -
Products: -
?
dihydroxyacetone + O2
3-hydroxy-2-oxo-propionaldehyde + H2O2
-
Substrates: best substrate for both intra- and extracellular enzymes
Products: -
Products: -
?
ganglioside + O2
? + H2O2
Polyporus circinatus
-
Substrates: bovine brain gangliosides in 70% n-propanol, in aqueous solution not a substrate
Products: -
Products: -
?
ganglioside + O2
? + H2O2
Polyporus circinatus
-
Substrates: gangliosides from bovine brain as free molecules and micellar or vesicular dispersions
Products: -
Products: -
?
guaran + O2
? + H2O2
-
Substrates: only intracellular enzyme
Products: -
Products: -
?
N-acetyl-D-galactosamine + O2
? + H2O2
Polyporus circinatus
-
Substrates: -
Products: -
Products: -
?
raffinose + O2
? + H2O2
-
Substrates: more rapidly oxidized than D-galactose
Products: -
Products: -
?
raffinose + O2
? + H2O2
-
Substrates: same activity as for D-galactose
Products: -
Products: -
?
raffinose + O2
? + H2O2
Polyporus circinatus
-
Substrates: more rapidly oxidized than D-galactose
Products: -
Products: -
?
stachyose + O2
? + H2O2
-
Substrates: oligosaccharides containing D-galactose at the nonreducing end are oxidized by the same mechanism as D-galactose
Products: -
Products: -
?
stachyose + O2
? + H2O2
-
Substrates: only intracellular enzyme
Products: -
Products: -
?
stachyose + O2
? + H2O2
Polyporus circinatus
-
Substrates: best substrate tested
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
one pyrroquinoline covalently bound to one molecule, additional two-electron redox center
Cys-Tyr cofactor
an inactive, oxidized state of FgrGalOx, which contains a Cu(II) site and a 1-electron reduced Cys-Tyr cofactor, produce a low-temperature EPR spectrum, this inactive state can be activated under typical assay conditions
-
Cys-Tyr cofactor
the enzyme contains a unique metalloradical complex consisting of a copper atom and a tyrosine residue covalently attached to the sulfur of a cysteine. The Tyr-Cys crosslink is essential for the catalytic activity of GalOx. The formation of the TyrN-Cys redox cofactor in GalOx is a self-processing reaction requiring only the apoprotein, copper, and dioxygen; no other proteins or enzymes are required for the processing and assembly of the catalytically active enzyme
-
Cys-Tyr cofactor
-
the active-site Cu is coordinated by a unique cysteinylated tyrosine (Cys-Tyr) ligand that serves as a second redox-active cofactor. Post-translational biogenesis of Cys-Tyr is copper- and O2-dependent, resulting in a self-processing enzyme system. Mechanism of cofactor biogenesis in galactose oxidase, overview. The role of cysteinylation (as well asPi-stacking of an adjacent conserved Trp) is to stabilize the (Cys-Tyr)radical and allow its function as a redox cofactor at a more biologically accessible potential. In turnover the Cu/(Cys-Tyr) unit accomplishes 2e- redox by shuttling between CuI/(Cys-Tyr)- and CuII/(Cys-Tyr) radical states in a ping-pong type mechanism
-
additional information
-
radical cofactor, the active site consists of two one-electron redox units involving residues Y495, H496, H581, Y272, and W290, a Cu2+ ion, and a crosslinked Y272-C228 radical cofactor, which together are responsible for the catalytic activity
-
additional information
-
mechanism of cofactor biogenesis, overview, metalloradical complex, comprised of a protein radical coordinated to a copper ion in the active site, the unusually stable protein radical is formed from the redox-active side chain of a cross-linked tyrosine residue, TyrCys
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
Cu3+
-
first evidence of oxidation by the Cu(III) enzyme with concomitant formation of a Cu(I) enzyme
Mn2+
additional information
copper
copper content: 1.2 mol of Cu per mol of wild-type enzyme, 0.96 mol of Cu per mol of mutant enzyme W290F, 1 mol Cu per mol of mutant enzyme W290G, 1.3 mol of Cu per mol of mutant enzyme W290H
copper
-
galactose oxidase is a copper-dependent enzyme that accomplishes 2e- substrate oxidation by pairing a single copper with an unusual cysteinylated tyrosine (Cys-Tyr) redox cofactor. The active site of GO contains only a single Cu . Post-translational biogenesis of Cys-Tyr is copper- and O2-dependent, resulting in a self-processing enzyme system. Cu(I) and Cu(II) enzyme states, Cu(I) active site modeling: on model uses the crystal structure of apo pre-processed GO (PDB ID 2VZ1) with Cu(I) manually added as the starting structure, while the other uses the crystal structure of processed Cu(II)-GO (PDB ID 1GOF) with the Cys-Tyr crosslink manually removed. In both cases, the model includes Cys228, Tyr272, Tyr495, His496 and His581 residues. Cu(I) activation mechanism, overview
Cu2+
-
metalloradical complex structure, overview, comprised of a protein radical coordinated to a copper ion in the active site, the coordination environment of the metal center is altered during redox and ligation changes in the active site
Cu2+
-
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
essentially required, binding site structure, residues Cys228 and Tyr272 in FgrGalOx are linked via a thioether bond. An inactive, oxidized state of FgrGalOx, which contains a Cu(II) site and a 1-electron reduced Cys-Tyr cofactor, produce a low-temperature EPR spectrum, this inactive state can be activated under typical assay conditions
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
-
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
-
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
the enzyme contains a unique metalloradical complex consisting of a copper atom and a tyrosine residue covalently attached to the sulfur of a cysteine
Cu2+
-
required, copper enzyme. The active site of the enzyme contains a tyrosine residue and a copper atom, and in the active form of galactose oxidase the tyrosine is in the radical form and the copper atom at oxidation state +2
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
-
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
a copper metalloenzyme, when fully reduced, the copper atom is at oxidation state +1 and can react with molecular oxygen to generate hydrogen peroxide
Cu2+
-
copper site with a thioether bond linking Cys228 and Tyr272 in a stacking interaction with Trp290, stabilizes the protein free-radical species essential for catalysis
Cu2+
-
the active site consists of two one-electron redox units involving residues Y495, H496, H581, Y272, and W290, a Cu2+ ion, and a crosslinked Y272-C228 radical cofactor, which together are responsible for the catalytic activity
Cu2+
-
essentially required, copper enzyme, removal of copper and free radicals inactivates the enzyme
Cu2+
metalloenzyme, copper catalytic centre of immobilzed enzyme, overview. 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) in the active site
additional information
addition of copper sulfate to shake-flask cultivations doubles mutant GaO-CBM29 activity, whereas enzyme production in a bioreactor system increases the yield of CBM29-GaO and GaO-CBM29 by more than 12times and 6times, respectively. Corresponding specific activities also increase by more than 20%. Addition of 0.5 mM copper (II) sulfate to reaction mixtures containing purified GaO, CBM29-GaO, and GaO-CBM29, or treatment with potassium ferricyanide, does not increase corresponding specific activities, confirming that the purified proteins are in the fully oxidized and active state
additional information
-
addition of copper sulfate to shake-flask cultivations doubles mutant GaO-CBM29 activity, whereas enzyme production in a bioreactor system increases the yield of CBM29-GaO and GaO-CBM29 by more than 12times and 6times, respectively. Corresponding specific activities also increase by more than 20%. Addition of 0.5 mM copper (II) sulfate to reaction mixtures containing purified GaO, CBM29-GaO, and GaO-CBM29, or treatment with potassium ferricyanide, does not increase corresponding specific activities, confirming that the purified proteins are in the fully oxidized and active state
additional information
GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site
additional information
no or poor effects by Mg2+, K+, Na+, NH4+, Mn2+, and NaF
additional information
-
no or poor effects by Mg2+, K+, Na+, NH4+, Mn2+, and NaF
additional information
-
the monomeric enzyme containing a mononuclear copper ionis coordinated with an unusually stable cysteinyl-tyrosine protein free radical, removal of copper and free radicals inactivates the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ganglioside
Polyporus circinatus
-
bovine brain and Tay-Sachs disease gangliosides: competitive inhibition
EDTA
inhibits the formation of the thioether bond under anaerobic conditions (posttranslational modification)
H2O2
-
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
H2O2
-
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
H2O2
-
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity; high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
H2O2
-
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
H2O2
high concentrations of hydrogen peroxide inactivate GAO, catalase can be added to the reaction mixture to degrade H2O2 and prolong GAO activity
N-bromosuccinimide
-
complete inactivation by oxidation of active center tryptophan
additional information
-
no inhibition: EDTA, Tween 80, NH4+, Na+, Mg2+, K+, and glycerol
-
additional information
-
in both active and inactive forms, protein monomer integrity is lost with a single radiation interaction anywhere in the polypeptide, but enzymatic activity is more resistant, yielding target sizes considerably smaller than that of the monomer
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K3[Fe(CN)6]
-
the inactive form of GOase can be reactivated by further reduction to form the active copper(I) complex or reformation of the radical by single-electron oxidation. In practice, only reoxidation, and not further reduction, of the inactive state is performed to ensure a fully active enzyme, typically using mild chemical oxidants such as potassium ferricyanide
additional information
-
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
-
substrate itself acts as a modifier, substrate activation
-
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
-
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
-
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
-
the inactive form ofGO can be oxidized to the active radical by peroxidases
-
additional information
-
the concentration and type of buffer is essential for the activity of GOase, which is significantly more active in sodium phosphate buffer than in other buffers investigated
-
additional information
-
protein based single-electron oxidants such as peroxidases can regenerate the active radical center of the enzyme
-
additional information
-
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
-
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
additional information
in the active form of GAO, the copper atom is at oxidation state +2 and the tyrosine is in a radical form. Reduction of the tyrosine radical generates the inactive form of GAO, which can be rescued by treating the inactive form with mild oxidants, such as, hexacyanoferrate (III), iridium (IV) chloride, molybdic cyanide, sodium periodate, potassium dichromate, or copper sulfate. Peroxidases can also enhance the action of GAO by oxidizing the inactive form to the active radical form
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Cell surface glycoprotein patterns of cell lines derived from human small cell carcinoma of the lung.
Carcinoma
Expression of the tumor marker D-galactose-beta-[1-->3]-N-acetyl-D-galactosamine by premalignant and malignant prostate.
Carcinoma
Histochemical and immunohistochemical study of human gastric carcinoma differentiation with special reference to supplementary role for endosonography in evaluating depth of invasion.
Carcinoma, Hepatocellular
Increased binding and killing of neuraminidase-galactose oxidase-treated tumor cells by normal macrophages.
Carcinoma, Small Cell
Cell surface glycoprotein patterns of cell lines derived from human small cell carcinoma of the lung.
Cholera
Correlation between macrophages and their membrane fraction. Cytocidal activities on neoplastic cells.
Cholera
Isolation of cholera toxin receptors from a mouse fibroblast and lymphoid cell line by immune precipitation.
Colonic Neoplasms
Detection of the tumor marker D-galactose-beta-(1-->3)-N-acetyl-D-galactosamine in colonic cancer and precancer.
Colorectal Neoplasms
Common expression of the tumor marker D-galactose-beta-[1-->3]-N-acetyl-D-galactosamine by different adenocarcinomas: evidence of field effect phenomenon.
Galactosemias
One-pot synthesis of the stable CdZnTeS quantum dots for the rapid and sensitive detection of copper-activated enzyme.
Graft vs Host Disease
A trial of alloreactive T-cell depletion using biotinylated galactose oxidase for the prevention of acute graft-versus-host diseases.
Herpes Simplex
Galactose-rich glycoproteins are on the cell surface of herpes virus-infected cells. 1. Surface labeling and serial lectin binding studies of Asn-linked oligosaccharides of glycoprotein gC.
Infections
Studies on malaria in Papua New Guinea: comparison of the surface glycoproteins on red blood cells from infected and uninfected individuals.
Infections
Suppression of the hypersensitive response in wheat stem rust interaction by reagents with affinity for wheat plasma membrane galactoconjugates.
Leukemia
Functional and partial chemical characterization of the carbohydrate moieties of the IgE receptor on rat basophilic leukemia cells and rat mast cells.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Aberrant sialylation of granulocyte membranes in chronic myelogenous leukemia.
Liver Neoplasms
Electrofluorochromic Imaging Analysis of Glycan Expression on Living Single Cell with Bipolar Electrode Arrays.
Malaria
Studies on malaria in Papua New Guinea: comparison of the surface glycoproteins on red blood cells from infected and uninfected individuals.
Mastocytoma
Induction of lymphocyte cytotoxicity by modification of the effector or target cells with periodate or with neuraminidase and galactose oxidase.
Melanoma
Cell surface glycoproteins of human tumor cell lines: unusual characteristics of malignant melanoma.
Neoplasms
Activation of human T lymphocytes I. Requirements for mitogen-induced proliferation of antigen-specific T lymphocyte clones.
Neoplasms
Common expression of the tumor marker D-galactose-beta-[1-->3]-N-acetyl-D-galactosamine by different adenocarcinomas: evidence of field effect phenomenon.
Neoplasms
Increased binding and killing of neuraminidase-galactose oxidase-treated tumor cells by normal macrophages.
Neoplasms
Relationship of gangliosides to the structure and function of thyrotropin receptors: their absence on plasma membranes of a thyroid tumor defective in thyrotropin receptor activity.
Rhabdomyosarcoma
Comparison of polypeptides from cultured human fibroblasts and sarcoma cells.
Rubella
Rubella virus contains one capsid protein and three envelope glycoproteins, E1, E2a, and E2b.
Stomach Neoplasms
Histochemical and immunohistochemical study of human gastric carcinoma differentiation with special reference to supplementary role for endosonography in evaluating depth of invasion.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics, isotope kinetics, kinetic analysis
-
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
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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1067
1-methyl-alpha-D-galactopyranoside
-
mutant C383S/Y436H/V494A, pH 7.0, 25°C
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
516.7
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant CBM29-GaO
600
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant GaO-CBM29
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
-
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.23
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant CBM29-GaO
9.93
D-galactose
pH 7.0, 30°C, recombinant chimeric enzyme mutant GaO-CBM29
20.31
galactoglucomannan
pH 7.0, 25°C, recombinant wild-type enzyme
30.64
galactoglucomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
45.05
galactoglucomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
23.02
galactoxyloglucan
pH 7.0, 25°C, recombinant wild-type enzyme
-
26.07
galactoxyloglucan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
60.09
galactoxyloglucan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
23.56
guar galactomannan
pH 7.0, 25°C, recombinant wild-type enzyme
-
64.4
guar galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
181.08
guar galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
22.63
locust bean galactomannan
pH 7.0, 25°C, recombinant wild-type enzyme
-
75.79
locust bean galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant CBM29-GaO
-
445.8
locust bean galactomannan
pH 7.0, 25°C, recombinant chimeric enzyme mutant GaO-CBM29
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
ganglioside
Polyporus circinatus
-
gangliosides in aqueous solution from Tay Sachs disease, competitive non-substrate inhibition
0.004
ganglioside
Polyporus circinatus
-
bovine brain gangliosides in aqueous solution, competitive non-substrate inhibition
0.12
ganglioside
Polyporus circinatus
-
bovine brain gangliosides in 70% n-propanol, competitive substrate inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
132 - 627
purified recombinant enzyme expressed from Pichia pastoris under different conditions, overview. pH and temperature not specified in the publication
159
purified recombinant His-tagged enzyme, substrate D-galactose, pH 7.0, 30°C
226
purified recombinant His-tagged enzyme, substrate 1-methyl-beta-D-galactopyranoside, pH 7.0, 30°C
61
purified recombinant His-tagged full-length enzyme, expressed from Pichia pastoris using the alpha-factor signal of Saccharomyces cerevisiae, pH 7.0, 40°C
63.2
purified recombinant His-tagged full-length enzyme, expressed from Pichia pastoris, pH 7.0, 40°C
65.4
purified recombinant His-tagged enzyme, expressed from Escherichia coli, pH 7.0, 40°C
additional information
-
enzyme activity in filtrates of the different isolates, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
two ionizable groups involved in catalysis with basic pH optima
additional information
-
two ionizable groups involved in catalysis with basic pH optima
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10.5
-
tested range, decrease of kcat/Km by 2 orders of magnitude compared to maximum kcat/Km
5.5 - 9
6 - 7
-
pH 6: about 80% of maximal activity, pH 7: about 25% loss of activity, oxidation of glycolaldehyde
6 - 9
5.5 - 9
activity range, more than 95% activity in the range of pH 6.0-7.5, profile overview. Inactive at pH 5.0 and below
6 - 9
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 65% of maximal activity
6 - 9
more than 80% of the maximum activity between pH 6.0 and 9.0, maximum activity occurs at pH 7.0 (phosphate buffer) and 8.0 (Tris buffer), respectively. At pH values below pH 5.0 the enzyme loses its activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
40
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 90% of maximal activity, 50°C: about 60% of maximal activity
40 - 60
-
40°C: about 65% of maximal activity, 60°C: about 80% of maximal activity, oxidation of glycolaldehyde
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
calculated from sequence
6.2
calculated from sequence
7.4
calculated from sequence
8.9
calculated from sequence
9.3
calculated from sequence
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Gibberella zeae, formerly Dactylium dendroides
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
maximum galactose oxidase production (approximately 4.0 U/ml) is obtained when fermentation is carried out at 25°C, with orbital shaking (100 rpm) and an initial medium of pH 7.0, for 96 h, using a 2% (v/v) inoculum made from a homogenized four-day-old liquid culture, in the presence of copper, manganese, and magnesium
brenda
developing anther
brenda
expression is strongest in late stages of anther development
brenda
-
-
389852, 389853, 389854, 389855, 389858, 389859, 389861, 389862, 389865, 389867, 389868, 389872, 389874, 389875, 389876, 389877, 389879
brenda
funiculus and septum
brenda
developing silique
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme is secreted to the apoplast late in the differentiation of seed coat epidermal cells
brenda
protein is secreted, and sequence presents N-terminal secretory and maturation sequences
-
brenda
-
-
-
brenda
-
broad specificity toward primary alcohols, especially toward the C-6 hydroxyl of galactopyranosides
-
brenda
-
intracellular enzyme possesses a more restricted substrate specificity than the extracellular form
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
physiological function
additional information
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
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 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
-
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
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
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
-
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
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
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
-
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
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
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
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 modeling based on the structure of GalOx from Fusarium graminearum
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GAOA_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
680
0
72791
Swiss-Prot
-
E6PBN6_GIBM7
Gibberella moniliformis (strain M3125 / FGSC 7600)
681
0
72777
TrEMBL
-
Q93Z02_ARATH
548
0
61071
TrEMBL
Mitochondrion (Reliability: 3)
Q9SVX6_ARATH
547
0
61026
TrEMBL
Secretory Pathway (Reliability: 3)
A0A024GZ97_9MICC
760
0
78863
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
65000
66000
68000
68500
recombinant galactose oxidase without the pro sequence, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 77000 and x * 74000, SDS-PAGE, x * 72500, calculated from sequence
monomer
1 * 72000, recombinant His-tagged enzyme, SDS-PAGE, structure analysis, overview
monomer
-
1 * 72000, recombinant His-tagged enzyme, SDS-PAGE, structure analysis, overview
-
monomer
-
1 * 68000, SDS-PAGE, sedimentation equilibrium in 7 M guanidine-HCl and 2-mercaptoethanol
additional information
the enzyme contains two domains, one is the N-terminal CBM32 domain, tertiary structure comparison
additional information
-
the enzyme contains two domains, one is the N-terminal CBM32 domain, tertiary structure comparison
additional information
trypsin digestion and peptide mapping, mass spectrometric analysis
additional information
-
trypsin digestion and peptide mapping, mass spectrometric analysis
-
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 modeling based on the structure of GalOx from Fusarium graminearum
-
additional information
-
the active site structure consists of two one-electron redox units involving residues Y495, H496, H581, Y272, and W290, a Cu2+ ion, and a crosslinked Y272-C228 radical cofactor, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
sequence contains no putative N-glycosylation sites
proteolytic modification
side-chain modification
copper-dependent formation of a C228-Y272 thioether bond, generation of the Y272 radical
glycoprotein
-
intracellular form highly glycosylated, extracellular form less glycosylated
proteolytic modification
cleavage of a secretion signal sequence, copper-dependent cleavage of an N-terminal pro sequence
proteolytic modification
-
to form mature active enzyme, the expressed pre-processed protein undergoes a series of post-translational modifications to remove leader peptides, and, most importantly, crosslink cysteine with tyrosine to form the Cys-Tyr cofactor
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the GAOV Cl2-Tyr272, and F2-Tyr272 incorporated variants at 1.48, 1.23, and 1.80 A resolution, respectively. Only one halogen atom remains in the cofactor. The structurally defined catalytic center with genetic unnatural tyrosine substitution is in the radical containing form as in the wild-type, i.e., Cu(II)-(Cl-Tyr radical-Cys) or Cu(II)-(F-Tyr radical-Cys). Thus an C-F/C-Cl bond cleavage is mediated by a mononuclear copper center
crystals of W290F and W290G are grown from protein as isolated, using hanging drop vapor diffusion from 1 to 2 M (NH4)2SO4 and 0.1 M sodium acetate at pH 4.0-5.0. To prepare the azide complex, wild-type galactose oxidase is dialyzed into 50 mM PIPES (pH 7.0) for 2 h, before addition of 20 mM sodium iethyl dithiocarbamate (DDC). The copper chelator DDC promotes the formation of orthorhombic crystals, which have more favorable crystal packing for substrate soaking experiments. The copper-free protein is crystallized in 13.5% PEG 8000, 200 mM calcium acetate, and 100 mM MES (pH 6.3)
sitting drop method. 2-5 mg/ml of enzyme mixed with equal volume of well solution. Crystals are soaked in oxygen-free Cu2+ solutions
wild-type enzyme and W290F mutant enzyme crystal structure analysis, PDB IDs 2EIE and 2EIC, respectively
analysis of crystal structure, PDB ID 1GOF, of the processed (cofactor formed) Cu(II) site reveals the active site ligation. Residues His496, His581, cysteinylated-Tyr272, and an acetate ion form the four equatorial ligands. In the structure of Cu(II)-GO crystallized without acetate, PDB ID 1GOG, the fourth equatorial position is occupied by a weakly bound water. A second tyrosine, Tyr495, occupies an axial position with a Cu-O 2.62.7 A distance in these structures. Spectroscopical characterization of the geometric structure of the pre-processed Cu(I) active site using Cu K-edge X-ray absorption spectroscopy. Molecular modeling of the pre-processed Cu(I)-galactose oxidase active site and biogenesis reaction coordinate
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
W290F
W290G
W290H
kcat/KM for D-galactose is 1180fold lower than wild-type value
C383S/Y436A
-
decrease in Km-value, decrease in kcat-value of 1-methyl-alpha-D-galactose, increase in kcat-value of D-galactose
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
W290F/R330K/Q406T
-
random mutagenesis, the mutant shows improved activity toward Glc compared to the wild-type enzyme
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
Y436H/V494A
-
slight decrease in kcat-value of 1-methyl-alpha-D-galactose, slight increase in kcat-value of D-galactose
C228G
additional information
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
-
the oxidized C228G mutant shows a higher reduction potential than the wild-type enzyme
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
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
-
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.5
-
intracellular form: 30% decrease of activity in 1 h, extracellular form: 50% decrease of activity in 1 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
the enzyme is completely stable for 120 h in buffer with stirring at 25°C, and the activity even increases 30% if the enzyme solution is also aerated in a similar experiment
30
40
40 - 60
the purified recombinant His-tagged enzyme shows half-lifes of 11.2 min, 5.3 min, and 2.7 min for incubation at 40°C, 50°C, and 60°C, respectively
50
60
70
additional information
the thermostability of GalOx from Fusarium oxysporum expressed in Escherichia coli is significantly lower than the thermostability of enzymes from other Fusarium strains
30
purified recombinant enzyme, pH 7.0, completely stable for at least 24 h
40
purified recombinant enzyme, pH 7.0, loss of 80% activity after 24 h
60
-
intracellular form more stable than extracellular form, stability is directly proportional to carbohydrate content
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to inactivation by guanidium-HCl, recovery of activity upon dilution
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.01 M phosphate buffer, pH 7.0, 0.1 mg/ml protein, 30% decrease of activity in 1 year
-
the enzyme is completely stable for 120 h in buffer with stirring at 25°C, and the activity even increases 30% if the enzyme solution is also aerated in a similar experiment
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of recombinant galactose oxidase under strict copper-free conditions
purification using immobilized biomimetic ligands or D(+)-galactosamine, two-step purification procedure using immobilized 1-amino-1-deoxy-beta-D-galactose
-
recombinant C-terminally His-tagged enzyme 28fold from Escherichia coli, recombinant C-terminally His-tagged full-length enzyme (including the native prepro signal sequence) 6fold from Pichia, and recombinant C-terminally His-tagged enzyme with alpha-factor signal sequence 22fold from Pichia pastoris
recombinant C-terminally His6-tagged enzyme 204fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant wild-type enzyme and chimeric enzyme mutants GaO-CBM29 and CBM29-GaO from Pichia pastoris strain KM71H by nickel affinity and hydrophobic interaction chromatography or vice-versa, follwed by dialysis and anion exchange chromatography
the commercially availbale enzyme is further purified by gel filtration
the enzyme from commercial preparation is further purified by gel filtration
-
to homogeneity, chromatography techniques
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
computational active-site models for galactose oxidase for the distinctive oxidation states (Cu2+ protein complex/radical), additional models including solvent molecules and second coordination sphere residues
-
functional expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3) cytoplasm, best in strain BL21 Star (DE3) at 25°C, induction for 4-6 h is optimal
-
gene gao, recombinant expression in in Aspergillus nidulans, Pichia pastoris, and Escherichia coli
gene gao, recombinant expression of wild-type enzyme and chimeric enzyme mutants GaO-CBM29 and CBM29-GaO in Pichia pastoris strain KM71H
gene gaoA, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene GAOA, sequence comparison to the Fusarium graminearum enzyne, sucessful recombinant expression of C-terminally His-tagged enzyme in Escherichia coli even without codon optimization or further amino acid substitutions. The C-terminal His-tag added to recombinant GalOx from Fusarium oxysporum does not interfere with the catalytic activity. Sucessful recombinant expression of C-terminally His-tagged full-length enzyme and enzyme with the alpha-factor signal sequence of Saccharomyces cerevisiae in Pichia pastoris
recombinant expression of C-terminally His-tagged enzyme in Pichia pastoris Mut+ strain PCE, under regulation of the AOX1 promoter, low exponential methanol feeding leads to 1.5fold higher volumetric productivity compared to high exponential feeding rates, culture condition and methanol feeding optimization, overview
recombinant expression of galactose oxidase without the pro sequence. Reaction with excess Cu2+ leads to formation of the C228-Y272 thioether bond both under aerobic and anaerobic conditions, the formation of the Y272 radical occures solely under aerobic conditions (posttranslational modifications)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
technology: creating hybrid-system by immobilization of GOase on gold electrode, technology enables creation of biosensors and biofuel cells and studying electrochemically the catalytic mechanism of reactions for which free radicals and electron-transfer reactions are involved
diagnostics
-
determination of galactose or lactose concentration in complex biological fluids by immobilized galactose oxidase
energy production
the enzyme is useful in fuel cells and the usage of biofuel cell with glucose
molecular biology
-
glycoprotein labeling using engineered variants of galactose oxidase, overview
synthesis
analysis
-
galactose oxidase adsorbed on, and covalently bound to, silica carriers is used for analytical determinations of D-galactose and galactose-containing sugars. Using a flowing oxygen electrode of the Clark-type, sensor system for enzymatic analysis of water solutions of galactose-containing carbohydrates is made. Measurements are taken both in the pulse and continuous modes of a substrate flowing through a column with an immobilized biocatalyst
analysis
-
galactose oxidase is an important component in electrochemical biosensors of galactose that are used for various biotechnology applications
analysis
-
a photoelectrochemical biosensor for quantitative detection of galactose is obtained immobilizing galactose oxidase on TiO2 nanorod arrays modified F-doped tin oxide (FTO) electrode. The direct electron transfer to galactose oxidase is achieved. The generated photocurrent of the stable platform is significantly enhanced after the addition of galactose in solution and the photocurrent intensity shows linear relationship with the galactose concentration. CaCl2, uric acid and ascorbic acid have no interference with the detection of galactose. The sensor can be reused and applied to measure the concentration of galactose in lactose-free milk
analysis
-
galactose oxidase adsorbed on, and covalently bound to, silica carriers is used for analytical determinations of D-galactose and galactose-containing sugars. Using a flowing oxygen electrode of the Clark-type, sensor system for enzymatic analysis of water solutions of galactose-containing carbohydrates is made. Measurements are taken both in the pulse and continuous modes of a substrate flowing through a column with an immobilized biocatalyst
-
synthesis
-
combination of UDP-Glc(NAc) 4'-epimerase and galactose oxidase in a one-pot synthesis of biotinylated nucleotide sugars. The enzymatic epimerization of uridine 5-diphospho-alpha-D-glucose and uridine 5-diphospho-N-acetyl-alpha-D-glucosamine and the subsequent oxidation of uridine 5-diphospho-alpha-D-galactose and uridine 5-diphospho-N-acetyl-alpha-D-galactosamine are combined with chemical biotinylation with biotin-epsilon-amidocaproylhydrazide in a one-pot synthesis. A mixture (1.0:1.4) of the biotinylated nucleotide sugars uridine 5-diphospho-6-biotin-epsilon-amidocaproylhydrazino-alpha-D-galactose and uridine 5-diphospho-6-biotin-epsilon-amidocaproylhydrazino-alpha-D-glucose, is produced in a reaction started with uridine 5-diphospho-alpha-D-glucose. One product, uridine 5-diphospho-6-biotin-epsilon-amidocaproylhydrazino-N-acetyl-alpha-D-galactosamine is formed when the reaction is initiated with uridine 5-diphospho-N-acetyl-alpha-D-glucosamine
synthesis
-
galactose oxidase is used as a catalyst to oxidize selectively the C-6 hydroxyls of terminal galactose to carbonyl groups, e.g. polysaccharides studied included spruce galactoglucomannan, guar galactomannan, larch arabinogalactan, corn fiber arabinoxylan, and tamarind seed xyloglucan, with terminal galactose. A multienzyme system is used, with catalase and horseradish peroxidase to enhance the action of galactose oxidase, GC-MS analysis, overview
synthesis
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. Increased substrate binding impeded the action of GaO fusions on more concentrated preparations of galactomannan, galactoglucomannan, and galactoxyloglucan
synthesis
-
galactose oxidase is a promising biocatalyst for the 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. GOase can be used to modify naturally occurring polysaccharides with terminal galactose moieties (or other saccharides through GOase mutants) by oxidizing the C6 hydroxyl groups and enabling further chemical or enzymatic modifications of the aldehyde such as amination. And GOase can be applied in the synthesis of a range of industrially relevant compounds containing ketones and aldehydes, such as diformylfuran obtained by selective oxidation of 5-hydroxymethylfurfural. GOase mutants able to enantioselectively oxidize secondary alcohols enable the use of the enzyme for kinetic resolution of racemic mixtures of secondary alcohols
synthesis
the enzyme can be used in the synthesis of small molecules, alcohols or amines, the production of H2O2 and reactive oxygen, and the production of O-glycosylated proteins
synthesis
Mn(OAc)3 functions as a suitable activator for several commercially available variants of GOase with a series of alcohol substrates. Use of the Mn(OAc)3 additive is also compatible with biocatalytic synthesis of islatravir and subsequent biocatalytic steps in the islatravir-forming cascade
synthesis
-
galactose oxidase is a promising biocatalyst for the 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. GOase can be used to modify naturally occurring polysaccharides with terminal galactose moieties (or other saccharides through GOase mutants) by oxidizing the C6 hydroxyl groups and enabling further chemical or enzymatic modifications of the aldehyde such as amination. And GOase can be applied in the synthesis of a range of industrially relevant compounds containing ketones and aldehydes, such as diformylfuran obtained by selective oxidation of 5-hydroxymethylfurfural. GOase mutants able to enantioselectively oxidize secondary alcohols enable the use of the enzyme for kinetic resolution of racemic mixtures of secondary alcohols
-
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Hypomyces rosellus
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Hypomyces rosellus
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1982
Polyporus circinatus
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1981
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1977
Hypomyces rosellus
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1977
Hypomyces rosellus
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1976
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1974
Hypomyces rosellus
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1974
Polyporus circinatus
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2004
Hypomyces rosellus
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Hypomyces rosellus
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2002
Fusarium sp.
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Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution
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2004
Fusarium sp., Fusarium sp. NRRL 2903
brenda
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433
227-239
2005
Aspergillus sp.
brenda
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Fusarium graminearum
-
brenda
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128
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2006
Hypomyces rosellus
brenda
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386
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2005
Fusarium fujikuroi
brenda
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349
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2007
Hypomyces rosellus
-
brenda
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23
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2007
Fusarium graminearum, Fusarium graminearum IMV-1060
brenda
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46
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2007
Fusarium graminearum (P0CS93)
brenda
Escalettes, F.; Turner, N.J.
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2008
Fusarium sp.
brenda
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Fusarium acuminatum
brenda
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2007
Paenibacillus sp. AIU 311
brenda
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Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen
Biochemistry
47
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2008
Fusarium graminearum (P0CS93)
brenda
Parikka, K.; Tenkanen, M.
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2009
Fusarium sp.
brenda
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Direct electron transfer to a metalloenzyme redox center coordinated to a monolayer-protected cluster
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131
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2009
Hypomyces rosellus
brenda
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Galactose oxidase as a model for reactivity at a copper superoxide center
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131
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2009
Hypomyces rosellus
brenda
Rokhsana, D.; Dooley, D.; Szilagyi, R.
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13
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2008
Hypomyces rosellus
brenda
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110
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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
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2011
Fusarium graminearum
brenda
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2012
Hypomyces rosellus
brenda
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2010
Fusarium sp.
brenda
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2011
Fusarium sp.
brenda
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2010
Hypomyces rosellus
brenda
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2016
Fusarium graminearum (P0CS93), Fusarium graminearum
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Fusarium graminearum (P0CS93), Fusarium graminearum, Fusarium graminearum SMD1168H (P0CS93)
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Hypomyces rosellus
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Fusarium verticillioides (E6PBN6), Fusarium subglutinans, Fusarium subglutinans (A0A0U1YLU5), Fusarium graminearum (P0CS93), Fusarium acuminatum, Fusarium konzum, Fusarium thapsinum, Fusarium nygamai, Fusarium verticillioides 7600 (E6PBN6)
-
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.
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2015
Fusarium graminearum (P0CS93), Fusarium graminearum
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2015
Fusarium sp., Fusarium sp. NRLL 2903
-
brenda
Paukner, R.; Staudigl, P.; Choosri, W.; Sygmund, C.; Halada, P.; Haltrich, D.; Leitner, C.
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9
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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
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108
73-79
2015
Fusarium sambucinum (A0A089QAB6), Fusarium sambucinum, Fusarium sambucinum MA1886 (A0A089QAB6)
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4
21939-21950
2014
Hypomyces rosellus (P0CS93)
-
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
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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
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75
538-544
2019
synthetic construct
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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
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142
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2020
Fusarium graminearum (P0CS93)
brenda
Yin, Z.; Zhi, J.
A photoelectrochemical biosensor based on the direct electron transfer to galactose oxidase
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397
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2020
Hypomyces rosellus
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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.
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61
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2019
Fusarium subglutinans (A0A0U1YLU5), Fusarium subglutinans
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Biocatalytic oxidation of alcohols using galactose oxidase and a manganese(III) activator for the synthesis of islatravir
Org. Biomol. Chem.
19
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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 (Q9M332), Arabidopsis thaliana (Q9LR03), Arabidopsis thaliana (Q9SVX6), Arabidopsis thaliana (Q9M9S1), Arabidopsis thaliana (F4K172), Arabidopsis thaliana (Q9FYG4)
brenda
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