EC Number |
Metals/Ions |
Reference |
---|
1.11.1.B2 | more |
enzyme contains no metal |
348334 |
1.11.1.B2 | vanadate |
- |
698914, 699774 |
1.11.1.B2 | vanadate |
the vanadate cofactor changes its protonation from quadruply protonated at pH 6.3 to triply protonated at pH 7.3 to doubly protonated at pH 8.3. In the mutant P395D/L241V/T343A, the vanadate protonation is the same at pH 5.0 and 8.3, and the cofactor is doubly protonated |
742747 |
1.11.1.B2 | Vanadium |
- |
674779 |
1.11.1.B2 | Vanadium |
dependent on |
725200 |
1.11.1.B2 | Vanadium |
enzyme contains vanadium |
657588 |
1.11.1.B2 | 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. Once the V-atom reacts with H2O2 and the peroxidovanadium(V) complex forms, a different coordination environment is formed which is critical for facilitation of the catalysis under mild conditions |
765199 |
1.11.1.B2 | Vanadium |
required, electronic structure of the vanadate protonation states, overview |
765248 |
1.11.1.B2 | Vanadium |
required, vanadium-dependent haloperoxidases (VHPOs) are not redox active at the vanadium metal center, remaining in the V5+ oxidation state, and thus do not require additional regeneration systems nor suffer oxidative inactivation during catalysis |
765333 |
1.11.1.B2 | Vanadium |
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Pervanadate is bound much more strongly to the enzyme than vanadate |
659641 |