1.1.3.9	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	685149	
1.1.3.9	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	742748	
1.1.3.9	Cu2+	-	389850, 389852, 389854, 389861, 389862, 389868, 389875, 389878, 696217, 699010	
1.1.3.9	Cu2+	0.4 mol copper per mol enzyme	389851	
1.1.3.9	Cu2+	0.95 g-atom per 68000 g of protein	389874, 389877	
1.1.3.9	Cu2+	1 atom copper per mol enzyme	389873, 389881	
1.1.3.9	Cu2+	1.2 mol per mol enzyme	389853	
1.1.3.9	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	743101	
1.1.3.9	Cu2+	a copper oxidase	741991	
1.1.3.9	Cu2+	a copper-dependent enzyme	743392	
1.1.3.9	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	389855	
1.1.3.9	Cu2+	copper-containing enzyme	672854	
1.1.3.9	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	743337	
1.1.3.9	Cu2+	essentially required, copper enzyme, removal of copper and free radicals inactivates the enzyme	726444	
1.1.3.9	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	743780	
1.1.3.9	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	671578	
1.1.3.9	Cu2+	required	674912	
1.1.3.9	Cu2+	required, copper enzyme	725202	
1.1.3.9	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	725175	
1.1.3.9	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	674186	
1.1.3.9	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	743642	
1.1.3.9	Cu3+	first evidence of oxidation by the Cu(III) enzyme with concomitant formation of a Cu(I) enzyme	389879	
1.1.3.9	Fe	1 atom iron per mol enzyme	389873	
1.1.3.9	Mg2+	5 mM, 107% of initial activity	763465	
1.1.3.9	Mn2+	1 mM, 1.6fold activation	687852	
1.1.3.9	Mn2+	marked increase of actvitiy at micromolar concentrations	389879	
1.1.3.9	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	741991	
1.1.3.9	additional information	GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site	743642	
1.1.3.9	additional information	no or poor effects by Mg2+, K+, Na+, NH4+, Mn2+, and NaF	743734	
1.1.3.9	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	726444