EC Number   |
Metals/Ions |
Reference |
|---|
   1.13.11.50 | Cu2+ |
sulfate, similar binding as Fe2+ in wild-type enzyme |
696107 |
| 1.13.11.50 | Fe2+ |
0.9-1.0 iron atoms per subunit, bound to active enzyme, essential for catalytic activity |
636327 |
| 1.13.11.50 | Fe2+ |
active site nonheme monoiron(II) center, facially ligated by three histidine residues, overview. Spectral analysis of Dke1 FeII-alpha-keto acid complexes with 4-hydroxyphneylpyruvate, overview |
725198 |
| 1.13.11.50 | Fe2+ |
Dke1 contains an atypical, three-histidine-ligated, mononuclear non-heme Fe2+ center, spectroscopic analysis, overview. Stabilizing effect of Glu98 on the 6C geometry of the metal center, priming it for substrate ligation. Also Thr107 stabilizes the Fe(II) cofactor |
711267 |
| 1.13.11.50 | Fe2+ |
essential for activity |
671683 |
| 1.13.11.50 | Fe2+ |
Fe2+-dependent enzyme, 1 molecule per subunit |
675466 |
| 1.13.11.50 | Fe2+ |
its active site consists of a redox-active iron(II) center |
764545 |
| 1.13.11.50 | Fe2+ |
nonheme Fe(II) cofactor, distinct organization of the hydrophilic triad in the free and substrate-ligated wild-type enzyme. In the free species, the Fe(II) center is coordinated to three histidines and one glutamate, whereas the substrate-ligated, catalytically competent enzyme-substrate complex has an Fe(II) center with three-histidine coordination, with a small fraction of three-histidine, one-glutamate coordination |
725553 |
| 1.13.11.50 | Fe2+ |
sulfate, necessary for enzyme activity. About 0.9 mol Fe2+/mol wild-type enzyme, less than 5% Fe2+ in mutants except 0.27 mol/mol H104E-enzyme and 0.45 mol/mol H104N-enzyme |
696107 |
| 1.13.11.50 | Fe2+ |
the Fe(II) coordinating triad is composed of three His residues, geometric and electronic structure of the Fe(II) center, structure and function comparison with other dioxygenases containing a two histidines and a carboxylate coordinating the iron center in a facial triad, overview |
711258 |
