1.1.3.9: galactose oxidase
This is an abbreviated version!
For detailed information about galactose oxidase, go to the full flat file.
Word Map on EC 1.1.3.9
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1.1.3.9
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neuraminidase
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copper
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borohydride
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lymphocyte
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lectin
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sialic
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tritiated
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mitogen
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concanavalin
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glycolipids
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galactosyl
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glycoconjugates
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agglutinin
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nab3h4
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ganglioside
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dendroides
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phenoxyl
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hydrazide
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sialylation
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borotritide
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graminearum
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one-electron
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sialoglycoproteins
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sialidase
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galactosamine
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copper-containing
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n-acetylgalactosaminyl
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desialylated
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naio4
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synthesis
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lactoperoxidase
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galactose-containing
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degradation
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diagnostics
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molecular biology
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energy production
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analysis
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biotechnology
- 1.1.3.9
- neuraminidase
- copper
- borohydride
- lymphocyte
- lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
- glycolipids
-
galactosyl
- glycoconjugates
- agglutinin
-
nab3h4
- ganglioside
- dendroides
-
phenoxyl
- hydrazide
-
sialylation
-
borotritide
- graminearum
-
one-electron
-
sialoglycoproteins
- sialidase
- galactosamine
-
copper-containing
-
n-acetylgalactosaminyl
-
desialylated
- naio4
- synthesis
- lactoperoxidase
-
galactose-containing
- degradation
- diagnostics
- molecular biology
- energy production
- analysis
- biotechnology
Reaction
Synonyms
AOd, At1g14430, At1g19900, At1g67290, At1g75620, At3g53950, At3g57620, At5g19580, beta-galactose oxidase, D-galactose oxidase, F5K20_250, FgrGalOx, galactose 6-oxidase, galactose oxidase, GalOx, GAO, GAOA, GAOX, GLOX1, Glox2, Glox3, GLOX4, GLOX5, GLOX6, GO, GOase, RUBY, RUBY PARTICLES IN MUCILAGE
ECTree
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Reaction
Reaction on EC 1.1.3.9 - galactose oxidase
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D-galactose + O2 = D-galacto-hexodialdose + H2O2
detailed mechanism, selective for pro-S hydrogen abstraction
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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
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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
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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
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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
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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
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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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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
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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
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