EC Number   |
Metals/Ions |
Reference |
|---|
   1.11.1.18 | vanadate |
in the solid state structure, every protein monomer binds one vanadate to the tele imidazole nitrogen of residue His486. In solutions of sodium orthovanadate, isoform apobromoperoxidase II recovers bromoperoxidase activity by one order of magnitude faster than apobromoperoxidase I |
726511 |
| 1.11.1.18 | Vanadium |
- |
765476 |
| 1.11.1.18 | Vanadium |
contains 0.3 vanadium ions per subunit |
671956 |
| 1.11.1.18 | Vanadium |
contains 0.38 vanadium ions per subunit |
671956 |
| 1.11.1.18 | Vanadium |
dependent on |
742111, 764730 |
| 1.11.1.18 | Vanadium |
enzyme contains vanadium |
671036, 672310, 673214 |
| 1.11.1.18 | Vanadium |
presence of vanadium coordinated to oxygen/nitrogen either as vanadium(V) (in the native, native plus bromide, and native plus peroxide samples) or vanadium(IV) (in the reduced enzyme). There are structural changes at the metal site on reduction of the native enzyme, notably a lengthening of the average inner-shell distance and the presence of terminal oxygen together with histidine and oxygen-donating residues |
671955 |
| 1.11.1.18 | Vanadium |
required vanadium as a transition metal ion that readily converts among oxidations states has the potential to support catalytic processes through oxidation/reduction chemistry as well as hydrolytic chemistry. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview |
765199 |
| 1.11.1.18 | Vanadium |
required, every monomer binds one equivalent of orthovanadate in a cavity formed from side chains of three histidines, two arginines, one lysine, serine, and tryptophan |
763808 |
| 1.11.1.18 | Vanadium |
requires vanadium for enzyme activity. The enzyme activity increases ca. 250% with the action of V5+ on the isolated enzyme, since more than 2/3 of the protein molecules are in the apo form. This effect of V5+ addition is inhibited in phosphate buffer, probably because phosphate and vanadate compete for the active site |
675244 |
