1.11.1.B2: chloride peroxidase (vanadium-containing)
This is an abbreviated version!
For detailed information about chloride peroxidase (vanadium-containing), go to the full flat file.
Word Map on EC 1.11.1.B2
-
1.11.1.B2
-
inaequalis
-
curvularia
-
vanadate
-
halide
-
bromoperoxidase
-
chlorination
-
vhpos
-
meroterpenoids
-
glucose-6-phosphatase
-
nodosum
-
ascophyllum
-
corallina
-
prenyltransferase
-
peroxo
-
vanadiumv
-
bipyramidal
-
seaweeds
-
td-dft
-
diagnostics
-
synthesis
- 1.11.1.B2
- inaequalis
-
curvularia
- vanadate
- halide
-
bromoperoxidase
-
chlorination
-
vhpos
-
meroterpenoids
- glucose-6-phosphatase
- nodosum
-
ascophyllum
-
corallina
- prenyltransferase
-
peroxo
-
vanadiumv
-
bipyramidal
- seaweeds
-
td-dft
- diagnostics
- synthesis
Reaction
Synonyms
chloroperoxidase, CPO, Mcl24, More, NapH1, PPHY, V-containing-haloperoxidase, vanadium chloroperoxidase, vanadium haloperoxidase, vanadium-containing chloroperoxidase, vanadium-containing peroxidase, vanadium-dependent chloroperoxidase, vanadium-dependent haloperoxidase, vCPO, VHPO
ECTree
1.11.1.B2 chloride peroxidase (vanadium-containing)Advanced search results
results (
results (Metals Ions
Metals Ions on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
vanadate
Vanadium
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
Vanadium
the vanadate binding pocket seems to form a very rigid frame stabilizing oxyanion binding
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
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
Vanadium
required, electronic structure of the vanadate protonation states, overview
Vanadium
the active-site vanadium(V) ion is linked to the protein via a histidine residue. Vanadium is a spectator ion that does not change its oxidation state during the reaction mechanism but holds and positions the H2O2 substrate and guides its proton-relay steps through its oxo and hydroxo ligands
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
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
