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
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sialylation
-
borotritide
- graminearum
-
one-electron
-
sialoglycoproteins
- sialidase
- galactosamine
-
copper-containing
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n-acetylgalactosaminyl
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desialylated
- naio4
- synthesis
- lactoperoxidase
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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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Application
Application on EC 1.1.3.9 - galactose oxidase
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analysis
biotechnology
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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
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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
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glycoprotein labeling using engineered variants of galactose oxidase, overview
synthesis
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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
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galactose oxidase is an important component in electrochemical biosensors of galactose that are used for various biotechnology applications
analysis
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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
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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
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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
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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
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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
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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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