EC Number   |
General Information |
Reference |
|---|
   1.11.1.18 | evolution |
chloroperoxidase (CPO) is a hybrid of two different families of enzymes, peroxidases and P450s |
764563 |
| 1.11.1.18 | evolution |
haloperoxidase enzymes (HPO) catalyze the oxidation of halides by hydrogen peroxide (H2O2) to form a hypohalite intermediate that can react rapidly with organic substrates to produce halogenated compounds or react with excess H2O2 to generate singlet oxygen (1O2). HPO can be classified according to the most electronegative halide they oxidize: chloroperoxidases (ClPO) oxidize chloride, bromide, and iodide, bromoperoxidases (BrPO) oxidize bromide and iodide, and iodoperoxidases (IPO) oxidize iodide. Haloperoxidases are generally metalloenzymes with either heme or vanadium cofactors, although enzymes not requiring a metal co-factor occur in some bacteria. Vanadium-bromoperoxidases (V-BrPO) appear to be the most common form of haloperoxidase in the marine environment |
-, 764730 |
| 1.11.1.18 | evolution |
the enzyme belongs into a class of metalloenzymes utilizing orthovanadate as a cofactor for activating hydrogen peroxide |
763808 |
| 1.11.1.18 | evolution |
vanadate-dependent haloperoxidases (VHPOs) are the enzymes that catalyze the 2e- oxidation of a halide by H2O2 to the corresponding hypohalous acids, HOX. Thereby, the formed HOX can react with a broad range of organic substrates to form a diverse variety of halogenated compounds. The classification of VHPOs is based on the nature of the halides oxidized, whereby when they catalyse the oxidation of Cl-, Br- or I- in the presence of H2O2, they are designated as chloroperoxidaes (CPOs), while for the oxidation of Br- or I- they are classified as bromoperoxidases (BPOs) and for the oxidation of I- as iodoperoxidases (IPOs) |
764543 |
| 1.11.1.18 | 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 |
| 1.11.1.18 | metabolism |
proposed pathways for the chloroperoxidase-catalyzed oxidation of phenol in the presence of bromide, overview |
764563 |
| 1.11.1.18 | more |
analysis of cofactor bonding and bromide oxidation at the active site, overview. Three-dimensional structure modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template |
763808 |
| 1.11.1.18 | more |
fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein |
764730 |
| 1.11.1.18 | more |
fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein. The APF assay cannot be used to detect iodoperoxidases (IPO) activity |
-, 764730 |
| 1.11.1.18 | more |
structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview |
765199 |
