EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
   1.11.1.18 | more |
production of polyhalogenated carbazoles (PHCs) from halogenation of carbazole in the presence of bromide and/or chloride under the catalysis of chloroperoxidase (CPO) isolated from the marine fungus Caldariomyces fumago, see also EC 1.11.1.10. A total of 25 congeners including mono-to tetra-substituted chlorinated, brominated, and mixed halogenated carbazoles (with substitution patterns of -BrCl, -BrCl2, -BrCl3, -Br2Cl, -Br2Cl2, and -Br3Cl) are produced from the reactions under various conditions. The PHC product profiles are apparently dependent on the halide concentrations. In the CPO-mediated chlorination of carbazole, 3-mono- and 3,6-dichlorocarbazoles predominated in the formation products. In addition to the less abundant mixed halogenated carbazoles (-Br2Cl), 1,3,6-tri- and 1,3,6,8-tetrabromocarbazoles are the dominant products in reactions containing both Br- and Cl- |
Leptoxyphium fumago |
? |
- |
- |
| 1.11.1.18 | more |
assay method development and evaluation: assay for BrPO (and ClPO) activity, based on the fluorescent probe, [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid [aminophenyl fluorescein (APF)], designed to selectively detect highly reactive oxygen species (hROS), overview. APF-based assays are used in different applications: (i) quantify the BrPO activity in two different species of diatom, Porosira glacialis and Fragilariopsis cylindrus, and (ii) measure BrPO activity in planktonic communities of coastal waters and investigate the size-distribution and temporal change of enzyme rates. In the APF assay, the hypohalite that generates fluorescein will potentially also react with other organic compounds if they are present, including molecules susceptible to electrophilic attack and halogenation. Bromoperoxidase concentration dependence of the dearylation of APF to fluorescein. The APF assay cannot be used to detect iodoperoxidases (IPO) activity |
Fragilariopsis cylindrus |
? |
- |
- |
| 1.11.1.18 | more |
assay method development and evaluation: assay for BrPO (and ClPO) activity, based on the fluorescent probe, [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid [aminophenyl fluorescein (APF)], designed to selectively detect highly reactive oxygen species (hROS), overview. APF-based assays are used in different applications: (i) quantify the BrPO activity in two different species of diatom, Porosira glacialis and Fragilariopsis cylindrus, and (ii) measure BrPO activity in planktonic communities of coastal waters and investigate the size-distribution and temporal change of enzyme rates. In the APF assay, the hypohalite that generates fluorescein will potentially also react with other organic compounds if they are present, including molecules susceptible to electrophilic attack and halogenation. Bromoperoxidase concentration dependence of the dearylation of APF to fluorescein. The APF assay cannot be used to detect iodoperoxidases (IPO) activity |
Porosira glacialis |
? |
- |
- |
| 1.11.1.18 | more |
assay method development and evaluation: assay for BrPO (and ClPO) activity, based on the fluorescent probe, [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid [aminophenyl fluorescein (APF)], designed to selectively detect highly reactive oxygen species (hROS), overview. APF-based assays are used in different applications: (i) to demonstrate the generation of highly reactive hypohalite by the partially purified V-BrPO of the red seaweed Corallina officinalis and to establish the temperature response and pH optima for V-BrPO of Corallina officinalis, and (ii) measure BrPO activity in planktonic communities of coastal waters and investigate the size-distribution and temporal change of enzyme rates. In the APF assay, the hypohalite that generates fluorescein will potentially also react with other organic compounds if they are present, including molecules susceptible to electrophilic attack and halogenation. Bromoperoxidase concentration dependence of the dearylation of APF to fluorescein. The APF assay cannot be used to detect iodoperoxidases (IPO) activity. The enzyme from Corallina officinalis is not active with iodide and chloride |
Corallina officinalis |
? |
- |
- |
| 1.11.1.18 | more |
CPO is a haeme-thiolate peroxidase requiring the presence of H2O2 to form an activated enzymatic species, responsible for oxidising either halides or organic substrates. CPO catalyses the halogenation of estrogens at comparable rates to other aromatic compounds. See also EC 1.11.1.10 |
Leptoxyphium fumago |
? |
- |
- |
| 1.11.1.18 | more |
H2O2 activation of the heme group. LC-MS/MS and gas chromatography-mass spectrometry (GC-MS) are used for product identification, overview. 2,2'-Dihyroxy-3,3',5,5'-tetrabromobiphenyl is also formed in the reactions, but is no substrate itself, no activity with 2,4,6-tribromophenol as a substrate. Evolution of BOC formation from phenol during CPO-mediated oxidation in the presence of bromide overview. Hydroxylated polybrominated diphenyl ethers (diOH-PBDEs) and hydroxylated polybrominated biphenyls (diOH-PBBs) formed by dihydroxyl group substitutions in the ortho-positions relative to the diphenyl ether bond or the single bond in biphenyl, may undergo intramolecular cyclization |
Leptoxyphium fumago |
? |
- |
- |
| 1.11.1.18 | more |
positional specificity of oxidative hydroxybromination for olefins, using rBPO-A1 and PA in the presence of methanol, is higher compared to a non-enzymatic reaction using peracetic acid. The oxidative bromination step, occurring after the enzymatic peroxidation step, is suggested to be pseudoenzymatic. Non-enzymatic oxidative bromination's influence can be disregarded under acidic condition of pH 6.0 or lower because generation of a strongly brominating active species is not the rate-limiting step under acidic conditions |
Kitasatospora aureofaciens |
? |
- |
- |
| 1.11.1.18 | more |
protein binding through the enzyme occurs primarily through hydrogen bridges and superimposed by Coulomb attraction according to thermochemical model on density functional level of theory. The strongest attractor is the arginine side chain mimic N-methylguanidinium, enhancing in positive cooperative manner hydrogen bridges toward weaker acceptors, such as residues from lysine and serine. Hydrogen peroxide activation occurs in the thermochemical model by side-on binding in orthovanadium peroxoic acid, oxidizing bromide with virtually no activation energy to hydrogen bonded hypobromous acid |
Ascophyllum nodosum |
? |
- |
- |
| 1.11.1.18 | more |
the disproportionation reaction of hydrogen peroxide is a bromidemediated reaction, i.e. V-BPO does not catalyze the formation of singlet oxygen in the absence of bromide ions |
Ascophyllum nodosum |
? |
- |
- |
| 1.11.1.18 | more |
vanadium containing bromoperoxidase mimicking (structural and/or functional) activities of vanadium(V) complexes has been reported by several groups in which the active site contains vanadium(V) coordinated to O/N donor ligands. Vanadium(V) complexes catalyze the oxidative bromination of organic substrates into useful halogenated organic compounds in the presence of halide and H2O2 in mild acid medium, just like natural VBrPO enzymes and hence, these are considered as models for VBrPO enzymes. Synthesis, crystal structure, DFT calculations, protein interaction, anticancer potential and bromoperoxidase mimicking activity of oxidoalkoxidovanadium(V) complexes: DFT calculations, protein interaction analysis, circular dichroism study, anticancer activity determination with MCF-7 cells, and determination of mitochondrial membrane potential (MMP) as well as intracellular reactive oxygen species (ROS) production, detailed overview |
Ascophyllum nodosum |
? |
- |
- |
