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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
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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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