EC Number |
Metals/Ions |
Reference |
---|
3.1.2.6 | Cd2+ |
the enzyme activity is increased by 23% and 53% at 0.25 and 0.5 mM Cd2+, respectively |
750861 |
3.1.2.6 | Co2+ |
glxII apoenzyme activity is regained |
692049 |
3.1.2.6 | Cobalt |
0.6 mol per mol of protein |
652537 |
3.1.2.6 | Fe2+ |
- |
652575 |
3.1.2.6 | Fe2+ |
0.26 mol per mol of enzyme |
664268 |
3.1.2.6 | Fe2+ |
0.8 mol per mol of protein, wild-type enzyme, 0.4 mol per mol of protein, R248W mutant enzyme |
650187 |
3.1.2.6 | Fe2+ |
behavior of Fe-GloB resembles that of Zn-GloB. Thiol-Fe bond is formed between the Cys moiety of glutathione and the metal site, the dinuclear iron sites show an enhanced antiferromagnetic coupling in the GloB-glutathione adduct. GloB-glutathione complex displays S-thiol-FeIII and S-thiol-FeII: charge transfer bands |
709398 |
3.1.2.6 | Fe2+ |
catalytic process of glyoxalase II involves a water moleule activated by a binuclear metal center containing one zinc atom plus a second bivalent metal ion which could be a zinc or an iron |
692048 |
3.1.2.6 | Fe2+ |
contains a binuclear Zn/Fe centre in its active site |
732633 |
3.1.2.6 | Fe2+ |
cytosolic isozyme, enzyme contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis, content of wild-type and mutant enzymes, overview |
652207 |