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
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galactosyl
- glycoconjugates
- agglutinin
-
nab3h4
- ganglioside
- dendroides
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phenoxyl
- hydrazide
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sialylation
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borotritide
- graminearum
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one-electron
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sialoglycoproteins
- sialidase
- galactosamine
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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
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1.1.3.9 galactose oxidaseAdvanced search results
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results (General Information
General Information on EC 1.1.3.9 - galactose oxidase
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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 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
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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
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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
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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
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metabolism
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copper-containing complexes, namely (benzoato-kappa2O,O')[(E)-2-({[2-(diethylamino)ethyl]imino}methyl)phenolato-kappa3N,N',O]copper(II) dihydrate, [Cu(C7H5O2)(C13H19N2O)] 2H2O, [(E)-2-({[2-(diethylamino)-ethyl]imino}methyl)phenolato-kappa3N,N',O](2-phenylacetato-kappa2O,O')copper(II), [Cu-(C8H7O2)(C13H19N2O)], and bis[my-(E)-2-({[3-(diethylamino)propyl]imino}-methyl)phenolato]-kappa4N,N',O:O;kappa4O:N,N',O-(my-2-methylbenzoato-kappa2O:O')copper(II) perchlorate, [Cu2(C8H7O2)(C12H17N2O)2]ClO4, have been tested for their activity in the oxidation of D-galactose. The results suggest that, unlike the enzyme galactose oxidase, due to the precipitation of Cu2O, this reaction is not catalytic
metabolism
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the indole ring, as an electron donor, stabilizes the phenoxyl radical by the pi-pi stacking interaction. A CuII complex of a methoxy-substituted salen-type ligand, containing a pendent indole ring on the dinitrogen chelate backbone exhibits the pi-pi stacking interaction of the indole ring mainly with one of the two phenolate moieties. The phenolate moiety in close contact with the indole moiety shows the characteristic phenoxyl radical structural features, indicating that the indole ring favors the pi-pi stacking interaction with the phenoxyl radical
physiological function
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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
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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
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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
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active site structure, analysis of crystal structure PDB ID 1GOF, overview. Molecular modeling of the pre-processed Cu(I)-galactose oxidase active site and biogenesis reaction coordinate
additional information
enzyme active site structure analysis of immobilzed enzyme, overview. In the active site region, the Cu ion is coordinated to two tyrosines (Tyr272 and Tyr495), two histidines (H496 and H581), and a solvent ligand (water), forming the inner coordination sphere (a type 2 centre). Importantly, Tyr272 is covalently bonded to Cys228 via a thioether bond and its radical form (Tyrc272) serves as a catalytic cofactor (i.e. the second redox site). Trp290 stacks over the Cys228 side chain and plays an essential role in generating Tyrc272 radicals for maintaining the enzyme catalytic cycles. Three-dimensional structure analysis
additional information
GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site
additional information
influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum
additional information
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influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum
additional information
the key active site residues of FgrGalOx, C228 and Y272, combine to form the unique crosslinked thioether-tyrosyl cofactor, and Y495, H496 and H581 that also coordinate to the copper ion. Another key active site is tryptophan W290in FgrGalOx. The N-terminal CBM32 domain binds galactosyl residues. Structure-function analysis of wild-type and mutant enzymes, overview
additional information
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the key active site residues of FgrGalOx, C228 and Y272, combine to form the unique crosslinked thioether-tyrosyl cofactor, and Y495, H496 and H581 that also coordinate to the copper ion. Another key active site is tryptophan W290in FgrGalOx. The N-terminal CBM32 domain binds galactosyl residues. Structure-function analysis of wild-type and mutant enzymes, overview
additional information
three-dimensional structure modeling based on the structure of GalOx from Fusarium graminearum
additional information
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three-dimensional structure modeling based on the structure of GalOx from Fusarium graminearum
additional information
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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
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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
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GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site
-
additional information
-
three-dimensional structure of GAO: a shallow active site and exposed single copper complex that likely enables access to different galactose containing substrates. As the catalysis involves two electron-transfer reactions, the enzyme carries a second cofactor, which is a tyrosine free radical. This radical is stabilized through a unique thioether bond between tyrosine (Tyr272) and cysteine (Cys228). The Tyr-Cys bridge acts as the ligand to the copper atom forming a stable metalloradical complex. In addition to the copper binding site in the C-terminal catalytic domain (domain 2), GAO harbours a distinct galactose binding domain at the N-terminus of the protein (domain 1)
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additional information
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three-dimensional structure modeling based on the structure of GalOx from Fusarium graminearum
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