EC Number   |
Metals/Ions |
Reference |
|---|
   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 | more |
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 | more |
GalOx is unusual among metalloenzymes in catalyzing a two-electron redox chemistry at a mononuclear metal ion active site |
743642 |
| 1.1.3.9 | more |
no or poor effects by Mg2+, K+, Na+, NH4+, Mn2+, and NaF |
743734 |
| 1.1.3.9 | more |
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 |
