The enzyme catalyzes the oxidation of halides in the presence of hydrogen peroxide to the corresponding hypohalous acids (PMID8552646). It uses a vanadium ion to perform the catalysis (PMID9165086).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| VO4 579 x | V | vanadium | vanadium | vanadate | Coordinates substrate Increases electrophilicity Electrostatic stabiliser |
*It refers to the MACiE reference pdb: 1vnc
| Metal/s Properties in Resting State | ||||||
| VO4 579 x | Resting state enzyme (1idu) | |||||
| Oxidation State | 5 | |||||
| Coordination Geometry | trigonalBipyramidal | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| References |
| -Hemrika W, Renirie R, Macedo-Ribeiro S, Messerschmidt A, Wever R Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His(496), Lys(353), Arg(360), and Arg(490). J Biol Chem. 1999 Aug 20;274(34):23820-7.(MEDLINE:10446144) |
| -Messerschmidt A, Prade L, Wever R Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form. Biol Chem. 1997 Mar-Apr;378(3-4):309-15.(MEDLINE:9165086) |
| - Some information have been also deduced from the MACiE mechanism model |