EC Number   |
General Information |
Reference |
|---|
   1.11.1.B2 | evolution |
vanadium-dependent haloperoxidases (VPXOs) are a class of enzymes that catalyze selective oxidation reactions for which vanadium is an essential cofactor converting halides to form halogenated organic products and water. These enzymes include chloroperoxidase and bromoperoxidase, which have very different protein sequences and sizes, but regardless the coordination environment of the active sites is constant. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview |
765199 |
| 1.11.1.B2 | metabolism |
the enzyme catalyzes a highly stereoselective chlorination-cyclization reaction in napyradiomycin antibiotic biosynthesis |
725200 |
| 1.11.1.B2 | metabolism |
VCPO Mcl24 is involved in halogenated meroterpenoid biosynthesis |
765333 |
| 1.11.1.B2 | metabolism |
VCPO NapH1 is involved in halogenated meroterpenoid biosynthesis |
765333 |
| 1.11.1.B2 | more |
calculation of higher protonation states and of a distict resting state for vanadium chloroperoxidase using quantum mechanics/molecular mechanics (QM/MM), with an atom-in-molecules analysis, overview. Di- and triprotonated states are identified as being candidates for the resting state based on a comparison of relative energies. The quadprotonated states as well as some of the triprotonated states are ruled out as the resting state. Structure of the active site of vanadium chloroperoxidase (VCPO) with bound vanadate cofactor in an unprotonated state |
765248 |
| 1.11.1.B2 | more |
structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview. The V-atom in the peroxidovanadium(V)-protein complex is in a distorted square pyramidal geometry (SPY-5) but the formation of this intermediate is clearly an important reason supporting the catalysis |
765199 |
| 1.11.1.B2 | more |
the active-site vanadium(V)-trioxo-hydroxo species is bound to His496. It is in trigonal bipyramidal symmetry and held in position with a string of polar (hydrogen-bonding) residues including those of Lys353, Arg360, Ser402, His404, and Arg490. As such, the active site is arranged in a tight hydrogen-bonding network, and a proton relay machinery appears to be available that can bring external protons into the active site to participate in the catalytic cycle. Active-site structure, overview. Computational modeling is performed using a combination of molecular mechanics (MM), molecular dynamics (MD), and density functional theory (DFT) calculations on cluster models. One narrow channel entering the active-site pocket with a cavity on the surface, where an organic substrate can attach. The channel connects the vanadium active site with the protein surface through the space in between the His404 and Arg490 residues. Consequently, hydrogen peroxide is inserted into the cavity at the end of the channel. Analysis of the catalytic cycle |
763783 |
| 1.11.1.B2 | more |
three-dimensional model of recombinant PPHY by homology modeling using the crystal structure of phytase chain A from Debaryomyces castellii (PDB ID 2gfiA) as template, inhibitor docking of sodium phytate, vanadate, and tartrate |
749608 |
| 1.11.1.B2 | physiological function |
enzyme is involved in the biosynthesis of the merochlorin meroterpenoid antibiotics |
741600 |
| 1.11.1.B2 | physiological function |
vanadium haloperoxidases are one of the few enzymes in nature that utilize a vanadium center and catalyze the halogenation of substrates through the biosynthesis of hypohalite. Vanadium chloroperoxidases (VCPOs) bind and activate hydrogen peroxide and in a reaction with chloride convert it into hypochlorite as a precursor for a substrate chlorination reaction |
763783 |
