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
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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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Cofactor
Cofactor on EC 1.1.3.9 - galactose oxidase
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pyrroloquinoline quinone
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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
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Cys-Tyr cofactor
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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
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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
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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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additional information
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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
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