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2,4-dibromophenol + bromide + H2O2
2,4,6-tribromophenol + 2 H2O
-
-
-
?
2-chloro-5,5-dimethyl-1,3-cyclohexane-dione HBr + H2O2
? + 2 H2O
2-chloro-5,5-dimethyl-1,3-cyclohexane-dione (mcd) is the standard substrate for the determination of haloperoxidase activity using H2O2 as the oxidant
-
-
?
2-chlorodimedone + chloride + H2O2
1,1-dimethyl-4,4-dichloro-3,5-cyclohexanedione + 2 H2O
model substrate monochlorodimedone, activity of EC 1.11.1.10
-
-
?
4-bromophenol + bromide + H2O2
2,4-dibromophenol + 2 H2O
-
-
-
?
beta-estradiol + bromide + H2O2
? + 2 H2O
-
-
-
?
beta-estradiol + chloride + H2O2
? + 2 H2O
-
-
-
?
Br- + H2O2 + (3E,6R,7R)-laurediol
deacetyllaurencin + H2O
-
-
-
-
?
Br- + H2O2 + (3R)-3-bromo-2,6-dimethylhept-5-en-2-ol
3,5-dibromo-2,6-dimethylheptane-2,6-diol + H2O
-
-
70% yield, at pH 6.0
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
bromochlorodimedone + ?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1-methoxynaphthalene
1-methoxy-4-bromonaphthalene + H2O
-
-
-
-
?
Br- + H2O2 + 1-phenylpent-4-en-1-ol
4-bromo-1-phenylpentane-1,5-diol + 5-bromo-1-phenylpentane-1,4-diol + 2-(bromomethyl)-5-phenyltetrahydrofuran + H2O
-
-
30% yield of 4-bromo-1-phenylpentane-1,5-diol, 28% yield of 5-bromo-1-phenylpentane-1,4-diol, and 25% yield of 2-(bromomethyl)-5-phenyltetrahydrofuran, at pH 6.0
-
?
Br- + H2O2 + 2,4,6-tribromophenol
1,3,6,8-tetrabromodibenzo-p-dioxin
-
formation of ppb-level yields of 1,3,6,8-tetrabromodibenzo-p-dioxin through direct condensation. Additionally, 1,3,7,9-tetrabromodibenzo-p-dioxin, 1,2,4,7-tetrabromodibenzo-p-dioxin, and/or 1,2,4,8-tetrabromodibenzo-p-dioxin and 1,3,7-tribromodibenzo-p-dioxin and 1,3,8-tribromodibenzo-p-dioxin are frequently formed but at lower yields. Reaction probably proceeds via bromine shifts or Smiles rearrangements, whereas the tribromodibenzo-p-dioxins may result from subsequent debromination processes
-
?
Br- + H2O2 + 2-hydroxybenzyl alcohol
2,4,6-tribromobenzyl alcohol + H2O
-
-
-
-
?
Br- + H2O2 + 2-methoxyphenol
2-bromo-6-methoxyphenol + 4-bromo-6-methoxyphenol + H2O
-
56% of product, in a 21/79 mixture of o-/p-regioisomers, plus 10% 2,4-dibromo-6-methoxyphenol
-
?
Br- + H2O2 + 2-methylphenol
2-bromo-6-methylphenol + 4-bromo-6-methylphenol + H2O
-
68% of product, in a 16/84 mixture of o-/p-regioisomers, plus 4% 2,4-dibromophenol
-
?
Br- + H2O2 + 2-t-butylphenol
2-bromo-6-t-butylphenol + 4-bromo-6-t-butylphenol + H2O
-
42% of product, in a 36/64 mixture of o-/p-regioisomers, plus 2% 2,4-dibromo-6-t-butylphenol
-
?
Br- + H2O2 + 4-pentynoic acid
(5E)-bromomethylidenetetrahydro-2-furanone
-
catalyzes the bromolactonization of 4-pentynoic acid forming (5E)-bromomethylidenetetrahydro-2-furanone. Formation of the bromofuranone likely results from an initial bromination reaction at the terminal alkyne, followed by cyclization from intermolecular nucleophilic attack by the terminal hydroxyl group
-
-
?
Br- + H2O2 + 5-methyl-1-phenylhex-4-en-1-ol
4-bromo-5-methyl-1-phenylhexane-1,5-diol + 2-(1-bromo-1-methylethyl)-5-phenyltetrahydrofuran + 3-bromo-2,2-dimethyl-6-phenyltetrahydro-2H-pyran + H2O
-
-
69% yield of 4-bromo-5-methyl-1-phenylhexane-1,5-diol, 6% yield of 2-(1-bromo-1-methylethyl)-5-phenyltetrahydrofuran, and 9% yield of 3-bromo-2,2-dimethyl-6-phenyltetrahydro-2H-pyran, at pH 6.0
-
?
Br- + H2O2 + aniline
o-bromoaniline + p-bromoaniline + ?
Br- + H2O2 + anisole
p-bromoanisole + o-bromoanisole + H2O
-
-
-
-
?
Br- + H2O2 + cyclohexene
trans-1-hydroxy-2-bromocyclohexane
-
-
-
-
?
Br- + H2O2 + cytidine
5-bromocytidine + H2O
-
-
-
-
?
Br- + H2O2 + cytosine
5-bromocytosine + H2O
-
-
-
-
?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 4-bromo-1H-pyrrole-2-carboxylate + methyl 5-bromo-1H-pyrrole-2-carboxylate + H2O
-
quantitative conversion within 24 h, 94% of product in 93/7 ratio of 4-/5-substituted regioisomers
-
?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 5-amino-4-bromocyclopenta-1,3-diene-1-carboxylate + methyl 5-amino-3-bromocyclopenta-1,3-diene-1-carboxylate + methyl 5-amino-3,4-dibromocyclopenta-1,3-diene-1-carboxylate + H2O
-
-
5% yield of methyl 5-amino-4-bromocyclopenta-1,3-diene-1-carboxylate, 59% yield of methyl 5-amino-3-bromocyclopenta-1,3-diene-1-carboxylate, and 5% yield of methyl 5-amino-3,4-dibromocyclopenta-1,3-diene-1-carboxylate, at pH 6.3 and 25°C
-
?
Br- + H2O2 + monochlorodimedon
?
-
-
-
?
Br- + H2O2 + monochlorodimedone
?
-
-
-
-
?
Br- + H2O2 + monochlorodimedone
? + H2O
Br- + H2O2 + monochlorodimedone
H2O + ?
-
-
-
-
?
Br- + H2O2 + monochlorodimedone
monobromo-monochlorodimedone + H2O
-
-
-
-
?
Br- + H2O2 + o-dianisidine
?
Br- + H2O2 + phenol
2,4,6-tribromophenol + H2O
-
-
-
-
?
Br- + H2O2 + phenol
2-bromophenol + 4-bromophenol + H2O
-
69% of product, in a 91/9 mixture of o-/p-regioisomers, plus 3% 2,4-dibromo-6-methylphenol and some 2,4,6-tribromophenol
-
?
Br- + H2O2 + phenol red
phenol blue + ?
-
-
-
-
?
Br- + H2O2 + pyrazole
4-bromopyrazole + H2O
-
-
-
-
?
Br- + H2O2 + styrene
DL-1 -bromo-2-hydroxy-2-phenylethane + H2O
-
-
-
-
?
Br- + H2O2 + thiophene
2-bromothiophene + H2O
-
-
-
-
?
Br- + H2O2 + trans-cinnamic acid
(+/-)-erythro-2-bromo-3-hydroxy-3-phenylpropionic acid + H2O
-
-
-
-
?
Br- + H2O2 + trans-cinnamyl alcohol
(+/-)-1,3-dihydroxy-2-bromo-3-phenylpropane + H2O
-
-
-
-
?
Br- + H2O2 + uracil
5-bromouracil + H2O
-
-
-
-
?
Capso + Br- + peracetic acid
?
carvacrol + chloride + H2O2
? + 2 H2O
-
-
-
?
cyclohexene + HBr + H2O2
? + 2 H2O
cytosine + Br- + peracetic acid
5-bromocytosine + ?
equiline + bromide + H2O2
? + 2 H2O
-
-
-
?
equiline + chloride + H2O2
? + 2 H2O
-
-
-
?
estradiol + 2 bromide + 2 H2O2
2,4-dibromo beta-estradiol + 4 H2O
-
-
-
?
estradiol + 2 chloride + 2 H2O2
2,4-dichloro beta-estradiol + 4 H2O
-
-
-
?
estradiol + bromide + H2O2
2-bromo beta-estradiol + 2 H2O
-
-
-
?
estradiol + bromide + H2O2
4-bromo beta-estradiol + 2 H2O
-
-
-
?
estradiol + chloride + H2O2
2-chloro beta-estradiol + 2 H2O
-
-
-
?
estradiol + chloride + H2O2
4-chloro beta-estradiol + 2 H2O
-
-
-
?
estrone + bromide + H2O2
? + 2 H2O
-
-
-
?
estrone + chloride + H2O2
? + 2 H2O
-
-
-
?
Hepes + Br- + peracetic acid
?
hesperetin + chloride + H2O2
? + 2 H2O
-
-
-
?
I- + H2O2 + monochlorodimedone
? + H2O
-
-
-
?
I- + H2O2 + o-dianisidine
?
I- + H2O2 + pyrazole
4-iodopyrazole + H2O
-
-
-
-
?
I- + H2O2 + uracil
5-iodouracil + H2O
-
-
-
-
?
indene + HBr + H2O2
? + 2 H2O
KBr + 2 H2O
KH + HBr + H2O2
-
-
-
?
monochlorodimedone + Br- + H2O2
?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
Mops + Br- + peracetic acid
5-bromocytosine + ?
naringenin + chloride + H2O2
? + 2 H2O
-
-
-
?
nerol + HBr + H2O2
? + 2 H2O
-
-
-
?
phenol + bromide + H2O2
4-bromophenol + 2 H2O
-
-
-
?
phenol + H2O2 + Br-
4-bromophenol + 2-bromophenol + H2O
-
-
4-bromophenol + 2-bromophenol at the ratio of 4:1
-
?
pyrene + chloride + H2O2
? + 2 H2O
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
RH + bromide + H2O2
RBr + 2 H2O
-
-
-
?
RH + HBr + H2O2
RBr + 2 H2O
RH + I- + H2O2 + H+
RI + 2 H2O
-
-
-
?
taurine + Br- + peracetic acid
bromotaurine + ?
Tes + Br- + peracetic acid
?
thymol + chloride + H2O2
? + 2 H2O
-
-
-
?
thymolsulfonphthalein + HBr + H2O2
? + 2 H2O
-
-
-
?
Tris + Br- + peracetic acid
?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
additional information
?
-
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone. Requirement of a catalytic triad in the halogenation mechanism
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + aniline
o-bromoaniline + p-bromoaniline + ?
-
no activity in absence of Br-
-
-
?
Br- + H2O2 + aniline
o-bromoaniline + p-bromoaniline + ?
-
in absence of Br- the enzyme oxidizes aniline via azobenzene and azoxybenzene finally into nitrobenzene
-
-
?
Br- + H2O2 + monochlorodimedone
? + H2O
-
-
-
?
Br- + H2O2 + monochlorodimedone
? + H2O
-
-
-
?
Br- + H2O2 + monochlorodimedone
? + H2O
-
-
-
?
Br- + H2O2 + monochlorodimedone
? + H2O
-
-
-
-
?
Br- + H2O2 + o-dianisidine
?
-
-
-
?
Br- + H2O2 + o-dianisidine
?
-
-
-
?
Capso + Br- + peracetic acid
?
-
-
-
-
?
Capso + Br- + peracetic acid
?
-
-
-
-
?
cyclohexene + HBr + H2O2
? + 2 H2O
-
-
-
?
cyclohexene + HBr + H2O2
? + 2 H2O
-
-
-
?
cytosine + Br- + peracetic acid
5-bromocytosine + ?
-
-
-
-
?
cytosine + Br- + peracetic acid
5-bromocytosine + ?
-
-
-
-
?
Hepes + Br- + peracetic acid
?
-
-
-
-
?
Hepes + Br- + peracetic acid
?
-
-
-
-
?
I- + H2O2
triiodide + ?
-
-
-
-
?
I- + H2O2
triiodide + ?
-
-
-
?
I- + H2O2 + o-dianisidine
?
-
-
-
?
I- + H2O2 + o-dianisidine
?
-
-
-
?
indene + HBr + H2O2
? + 2 H2O
-
-
-
?
indene + HBr + H2O2
? + 2 H2O
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
-
?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
-
-
-
?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0
-
-
?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0
-
-
?
Mops + Br- + peracetic acid
5-bromocytosine + ?
-
-
-
-
?
Mops + Br- + peracetic acid
5-bromocytosine + ?
-
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
-
?
RH + HBr + H2O2
RBr + 2 H2O
-
-
-
?
RH + HBr + H2O2
RBr + 2 H2O
-
-
-
?
RH + HBr + H2O2
RBr + 2 H2O
-
-
-
?
taurine + Br- + peracetic acid
bromotaurine + ?
-
-
-
-
?
taurine + Br- + peracetic acid
bromotaurine + ?
-
-
-
-
?
Tes + Br- + peracetic acid
?
-
-
-
-
?
Tes + Br- + peracetic acid
?
-
-
-
-
?
Tris + Br- + peracetic acid
?
-
-
-
-
?
Tris + Br- + peracetic acid
?
-
-
-
-
?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
the conversion of non-fluorescent APF to fluorescein through the production of HOBr by V-BrPO of is shown by increases in fluorescence following the addition of H2O2 to the enzyme assay mixture at approximately 50 s after initiation of data collection
-
-
?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
-
-
-
-
?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
-
-
-
-
?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
-
-
-
-
?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
-
-
-
-
?
additional information
?
-
enzyme uses hydrogen peroxide and bromide yielding molecular bromine as reagent for electrophilic hydrocarbon bromination
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
plays an important role in eliminating epiphytic organisms, especially microalgae on the surface. The activity increased during winter and spring and peaked in late spring. Functions to eliminate H2O2 compensating for catalase
-
-
?
additional information
?
-
-
strong brominating aactivity, weak chlorinating and iodating activities, catalyzes both benzylic and aromatic hydroxylations (e.g., of toluene and naphthalene)
-
-
?
additional information
?
-
-
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
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additional information
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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
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additional information
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the alkyl hydroperoxides ethyl hydroperoxide, cuminyl hydroperoxide, and tert-butyl hydroperoxide do not support bromination of dioxygen formation catalyzed by V-BrPO
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no substrate: chloride
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no substrate: chloride
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the natural brominated compound is dibromoacetaldehyde
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the natural brominated compound is dibromoacetaldehyde
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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
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additional information
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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
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additional information
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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
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additional information
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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-
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additional information
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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
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additional information
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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
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additional information
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the alkyl hydroperoxides ethyl hydroperoxide, cuminyl hydroperoxide, and tert-butyl hydroperoxide do not support bromination of dioxygen formation catalyzed by V-BrPO
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additional information
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no activity with Cl-
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additional information
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no activity with Cl-
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additional information
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the lowest specific bromoperoxidase activity occurs during the midexponential phase of growth and then increases steeply during the late stationary phase, suggesting that bromoperoxidase production is part of secondary metabolism
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additional information
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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
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additional information
?
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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
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additional information
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the role of the enzyme is related to its activity as a catalase rather than as a halogenatingt agent
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additional information
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no substrate: chloride
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additional information
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no substrate: chloride
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additional information
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no substrate: chloride
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additional information
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besides its phytase activity (EC 3.1.3.8) with myo-inositol hexakisphosphate, the enzyme rSt-Phy also shows haloperoxidase activity. Enzyme rSt-Phy brings out a change in color of phenol red from red-orange to blue-violet in the presence of metavanadate ions, H2O2 and KBr in the reaction mixture, which confirms the bromoperoxidation of phenol red. Only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, when vanadate ion is incorporated into the active site. Vanadate is a phosphate analogue, which is generally considered to bind as a transition state analogue to the phosphoryl transfer enzymes and inhibits their activities
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metabolism
proposed pathways for the chloroperoxidase-catalyzed oxidation of phenol in the presence of bromide, overview
evolution
chloroperoxidase (CPO) is a hybrid of two different families of enzymes, peroxidases and P450s
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
evolution
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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
evolution
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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
evolution
the enzyme belongs into a class of metalloenzymes utilizing orthovanadate as a cofactor for activating hydrogen peroxide
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)
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
evolution
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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
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evolution
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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
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physiological function
bromoperoxidase and chloroperoxidase enzymes catalyze the reaction between hydrogen peroxide and halides to generate highly reactive hypohalite intermediates able to dearylate APF. Haloperoxidases may play a role in algal-bacterial interactions
physiological function
chloroperoxidase (CPO) is a heme-thiolate enzyme able to catalyse the halogenation and oxidation of a wide range of organic substrates. CPO-catalysed chlorination and bromination reaction of natural estrogens, beta-estradiol, estrone and equiline are efficiently converted to halogenated compounds in the presence of chloride or bromide and hydrogen peroxide. The bromination reaction proceeds more efficiently than the chlorination reaction. Three major products are detected for chlorination of beta-estradiol, two of them are monohalogenated compounds while a third product is a dihalogenated compound at positions 2 and 4 of the aromatic ring A. Chlorinated compounds are not substrates for tyrosinase, suggesting that the halogenated form of estrogens is less susceptible to form o-quinones. Chlorinated estradiol is not a substrate of tyrosinase. Whereas E2 is completely consumed in the presence of tyrosinase, E2-derived chlorinated compounds are not transformed. 2,4-Dichloroestradiol is 90fold less estrogenic compared to beta-estradiol
physiological function
chloroperoxidase (CPO), secreted by the marine fungus Caldariomyces fumago, is a versatile enzyme with the capacity to catalyze the incorporation of halogen atoms into organic molecules in the presence of peroxides such as H2O2. 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. CPO-catalyzed halogenation of carbazole may play an important role in the natural formation of PHCs. PHCs exhibit dioxin-like toxicity and are persistent and bioaccumulative. PHCs induce cytochrome P450 enzymes and certain other enzyme activities. The chlorinated and brominated carbazoles produced in the reactions with Cl- and Br- in vitro are also found in aquatic environments, overview
physiological function
containing both a P450-like proximal pocket and a peroxidase-like distal pocket, enzyme chloroperoxidase (CPO) is a versatile heme-containing enzyme that possesses the catalytic capacities of both peroxidase and P450 enzyme families. CPO has multiple catalytic functions, attributable to four CPO-mediated processes, including bromination, radical coupling, intramolecular cyclization and debromination. Phenol is readily transformed into a variety of brominated organic compounds (BOCs) via the CPO-mediated oxidative process. Higher bromide concentrations and lower pH conditions both facilitate the formation of brominated products. While a higher bromination capacity is observed in pH 3.0 solutions, CPO-mediated radical couplings are more favorable at pH 5.0 and pH 6.0. Although CPO might catalyze chlorination when chloride and bromide coexisted in the solution, BOCs are the dominant products of CPO-mediated phenol oxidation. Bromination (EC 1.11.1.18) is preferable to chlorination (EC 1.11.1.10) in the CPO-mediated reaction in the presence of both bromide and chloride. Proposed pathways for the chloroperoxidase-catalyzed oxidation of phenol in the presence of bromide, overview
physiological function
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diatoms may play an important contribution to the control of H2O2 concentrations in natural seawater. Bromoperoxidase and chloroperoxidase enzymes catalyze the reaction between hydrogen peroxide and halides to generate highly reactive hypohalite intermediates able to dearylate APF. Haloperoxidases may play a role in algal-bacterial interactions
physiological function
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diatoms may play an important contribution to the control of H2O2 concentrations in natural seawater. Bromoperoxidase and chloroperoxidase enzymes catalyze the reaction between hydrogen peroxide and halides to generate highly reactive hypohalite intermediates able to dearylate APF. Haloperoxidases may play a role in algal-bacterial interactions
physiological function
the peroxide is the terminal oxidant for converting bromide into electrophilic bromine compounds
physiological function
vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions
physiological function
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diatoms may play an important contribution to the control of H2O2 concentrations in natural seawater. Bromoperoxidase and chloroperoxidase enzymes catalyze the reaction between hydrogen peroxide and halides to generate highly reactive hypohalite intermediates able to dearylate APF. Haloperoxidases may play a role in algal-bacterial interactions
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physiological function
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diatoms may play an important contribution to the control of H2O2 concentrations in natural seawater. Bromoperoxidase and chloroperoxidase enzymes catalyze the reaction between hydrogen peroxide and halides to generate highly reactive hypohalite intermediates able to dearylate APF. Haloperoxidases may play a role in algal-bacterial interactions
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additional information
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
additional information
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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
additional information
fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein
additional information
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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
additional information
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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
additional information
structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview
additional information
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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
-
additional information
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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
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Brindley, A.A.; Dalby, A.R.; Isupov, M.N.; Littlechild, J.A.
Preliminary X-ray analysis of a new crystal form of the vanadium-dependent bromoperoxidase from Corallina officinalis
Acta Crystallogr. Sect. D
54
454-457
1998
Corallina officinalis
brenda
Hofrichter, M.; Ullrich, R.
Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance
Appl. Microbiol. Biotechnol.
71
276-288
2006
Cyclocybe aegerita
brenda
Itoh, N.; Morinaga, N.; Kouzai, T.
Oxidation of aniline to nitrobenzene by nonheme bromoperoxidase
Biochem. Mol. Biol. Int.
29
785-791
1993
Pseudomonas putida, Corallina pilulifera
brenda
Sheffield, D.J.; Mort, A.J.; Harry, T.; Smith, A.J.; Rogers, L.J.
Bromoperoxidase of the macroalga Corallina officinalis
Biochem. Soc. Trans.
20
284S
1992
Corallina officinalis
brenda
Sheffield, D.J.; Smith, A.J.; Harry, T.R.; Rogers, L.J.
Thermostability of the vanadium bromoperoxidase from Corallina officinalis
Biochem. Soc. Trans.
21
445S
1993
Corallina officinalis
brenda
Arber, J.M.; de Boer, E.; Garner, C.D.; Hasnain, S.S.; Wever, R.
Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum
Biochemistry
28
7968-7973
1989
Ascophyllum nodosum
brenda
Soedjak, H.S.; Butler, A.
Characterization of vanadium bromoperoxidase from Macrocystis and Fucus: reactivity of vanadium bromoperoxidase toward acyl and alkyl peroxides and bromination of amines
Biochemistry
29
7974-7981
1990
Macrocystis pyrifera, Fucus distichus
brenda
Tromp, M.G.; Olafsson, G.; Krenn, B.E.; Wever, R.
Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum
Biochim. Biophys. Acta
1040
192-198
1990
Ascophyllum nodosum
brenda
Pelletier, I.; Altenbuchner, J.; Mattes, R.
A catalytic triad is required by the non-heme haloperoxidases to perform halogenation
Biochim. Biophys. Acta
1250
149-157
1995
Pseudomonas fluorescens
brenda
Krenn, B.E.; Plat, H.; Wever, R.
Purification and some characteristics of a non-haem bromoperoxidase from Streptomyces aureofaciens
Biochim. Biophys. Acta
952
255-260
1988
Kitasatospora aureofaciens
brenda
Rorrer, G.L.; Tucker, M.P.; Cheney, D.P.; Maliakal, S.
Bromoperoxidase activity in microplantlet suspension cultures of the macrophytic red alga Ochtodes secundiramea
Biotechnol. Bioeng.
74
389-395
2001
Ochtodes secundiramea
brenda
Butler, A.
Vanadium haloperoxidases
Curr. Opin. Chem. Biol.
2
279-285
1998
Corallina officinalis, Ascophyllum nodosum
brenda
Itoh, N.; Hasan, A.K.; Izumi, Y.; Yamada, H.
Substrate specificity, regiospecificity and stereospecificity of halogenation reactions catalyzed by non-heme-type bromoperoxidase of Corallina pilulifera
Eur. J. Biochem.
172
477-484
1988
Corallina pilulifera
brenda
Garcia-Rodriguez, E.; Ohshiro, T.; Aibara, T.; Izumi, Y.; Littlechild, J.
Enhancing effect of calcium and vanadium ions on thermal stability of bromoperoxidase from Corallina pilulifera
J. Biol. Inorg. Chem.
10
275-282
2005
Corallina pilulifera
brenda
Zeiner, R.; van Pee, K.H.; Lingens, F.
Purification and partial characterization of multiple bromoperoxidases from Streptomyces griseus
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134
3141-3149
1988
Streptomyces griseus, Streptomyces griseus Tu6
brenda
Knoch, M.; van Pee, K.H.; Vining, L.C.; Lingens, F.
Purification, properties and immunological detection of a bromoperoxidase-catalase from Streptomyces venezuelae and from a chloramphenicol-nonproducing mutant
J. Gen. Microbiol.
135
2493-2502
1989
Streptomyces venezuelae
brenda
Weng, M.; Pfeifer, O.; Krauss, S.; Lingens, F.; van Pee, K.H.
Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762
J. Gen. Microbiol.
137
2539-2546
1991
Kitasatospora aureofaciens
brenda
Pfeifer, O.; Pelletier, I.; Altenbuchner, J.; van Pee, K.H.
Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762
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138
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1992
Kitasatospora aureofaciens (P29715), Kitasatospora aureofaciens
brenda
Hara, I.; Sakurai, T.
Isolation and characterization of vanadium bromoperoxidase from a marine macroalga, Ecklonia stolonifera
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72
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1998
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Rehder, D.; Schulzke, C.; Dau, H.; Meinke, C.; Hanss, J.; Epple, M.
Water and bromide in the active center of vanadate-dependent haloperoxidases
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80
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2000
Ascophyllum nodosum
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Carter, J.N.; Beatty, K.E.; Simpson, M.T.; Butler, A.
Reactivity of recombinant and mutant vanadium bromoperoxidase from the red alga Corallina officinalis
J. Inorg. Biochem.
91
59-69
2002
Corallina officinalis (Q8LLW7)
brenda
Pelletier, I.; Pfeifer, O.; Altenbuchner, J.; van Pee, K.H.
Cloning of a second non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification
Microbiology
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Kitasatospora aureofaciens
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Streptomyces venezuelae
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Vanadium haloperoxidases from brown algae of the Laminariaceae family
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Saccharina latissima, Laminaria hyperborea
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Physiological function of bromoperoxidase in the red marine alga, Corallina pilulifera: production of bromoform as an allelochemical and the simultaneous elimination of hydrogen peroxide
Phytochemistry
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Corallina pilulifera
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Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the recombinant enzyme
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Corallina pilulifera
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The dodecameric vanadium-dependent haloperoxidase from the marine algae Corallina officinalis: Cloning, expression, and refolding of the recombinant enzyme
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Corallina officinalis
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A vanadium-dependent bromoperoxidase in the marine red alga Kappaphycus alvarezii (Doty) Doty displays clear substrate specificity
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Kappaphycus alvarezii, Kappaphycus alvarezii Doty
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Ascophyllum nodosum (P81701)
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51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases
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Ascophyllum nodosum (P81701)
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Ascophyllum nodosum
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Ascophyllum nodosum
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Kitasatospora aureofaciens (P29715), Kitasatospora aureofaciens
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Delisea pulchra
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Corallina officinalis (Q8LLW7)
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Ascophyllum nodosum (P81701)
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Ascophyllum nodosum (P81701), Ascophyllum nodosum
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Laurencia nipponica
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Thermothelomyces thermophilus (V5M269)
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X-ray diffraction and density functional theory provide insight into vanadate binding to homohexameric bromoperoxidase II and the mechanism of bromide oxidation
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Ascophyllum nodosum (K7ZUA3), Ascophyllum nodosum
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China, H.; Ogino, H.
A useful propionate cofactor enhancing activity for organic solvent-tolerant recombinant metal-free bromoperoxidase (perhydrolase) from Streptomyces aureofaciens
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Kitasatospora aureofaciens (P33912), Kitasatospora aureofaciens, Kitasatospora aureofaciens ATCC 10762 (P33912)
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Debnath, M.; Dolai, M.; Pal, K.; Bhunya, S.; Paul, A.; Lee, H.M.; Ali, M.
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Ascophyllum nodosum (K7ZUA3)
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Wang, K.; Huang, X.; Lin, K.
Multiple catalytic roles of chloroperoxidase in the transformation of phenol products and pathways
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Leptoxyphium fumago (P04963)
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Chen, Y.; Lin, K.; Chen, D.; Wang, K.; Zhou, W.; Wu, Y.; Huang, X.
Formation of environmentally relevant polyhalogenated carbazoles from chloroperoxidase-catalyzed halogenation of carbazole
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Leptoxyphium fumago (P04963)
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Archer, S.; Posman, K.; DeStefano, J.; Harrison, A.; Ladina, A.; Cheff, E.; Witt, D.
Fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein
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Fragilariopsis cylindrus, Porosira glacialis, Corallina officinalis (Q8LLW7), Porosira glacialis CCMP651, Fragilariopsis cylindrus CCMP3323
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McLauchlan, C.C.; Murakami, H.A.; Wallace, C.A.; Crans, D.C.
Coordination environment changes of the vanadium in vanadium-dependent haloperoxidase enzymes
J. Inorg. Biochem.
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2018
Ascophyllum nodosum (P81701)
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Undiano, E.; Roman, R.; Miranda-Molina, A.; Ayala, M.
Halogenation of estrogens catalysed by a fungal chloroperoxidase
Nat. Prod. Res.
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Leptoxyphium fumago (P04963)
brenda
Biswal, D.; Pramanik, N.; Drew, M.; Jangra, N.; Maurya, M.; Kundu, M.; Sil, P.; Chakrabarti, S.
Synthesis, crystal structure, DFT calculations, protein interaction, anticancer potential and bromoperoxidase mimicking activity of oxidoalkoxidovanadium(V) complexes
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2019
Ascophyllum nodosum (P81701)
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