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Literature summary for 1.11.1.18 extracted from
- Fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein (2019), Front. Mar. Sci., 6, 68 .
No PubMed abstract available
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NaN3 | the activity of V-BrPO is inhibited or inactivated by NaN3 | Corallina officinalis |  |
| NaN3 | the activity of V-BrPO is inhibited or inactivated by NaN3 | Fragilariopsis cylindrus | |
| NaN3 | the activity of V-BrPO is inhibited or inactivated by NaN3 | Porosira glacialis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Vanadium | dependent on | Corallina officinalis | |
| Vanadium | dependent on | Fragilariopsis cylindrus | |
| Vanadium | dependent on | Porosira glacialis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| RH + Br- + H2O2 + H+ | Corallina officinalis | - |
RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | Fragilariopsis cylindrus | - |
RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | Porosira glacialis | - |
RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | Porosira glacialis CCMP651 | - |
RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | Fragilariopsis cylindrus CCMP3323 | - |
RBr + 2 H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corallina officinalis | Q8LLW7 | - |
- |
| Fragilariopsis cylindrus | - |
a cold-water diatom | - |
| Fragilariopsis cylindrus CCMP3323 | - |
a cold-water diatom | - |
| Porosira glacialis | - |
a cold-water diatom | - |
| Porosira glacialis CCMP651 | - |
a cold-water diatom | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | lyophilized powder | Corallina officinalis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| monochlorodimedone + HBr + H2O2 | - |
Corallina officinalis | monobromomonochlorodimenone + 2 H2O | - |
? | |
| 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 | Fragilariopsis cylindrus | ? | - |
- |
|
| 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 | Porosira glacialis | ? | - |
- |
|
| 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 | Corallina officinalis | ? | - |
- |
|
| 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 | Porosira glacialis CCMP651 | ? | - |
- |
|
| 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 | Fragilariopsis cylindrus CCMP3323 | ? | - |
- |
|
| RH + Br- + H2O2 + H+ | - |
Corallina officinalis | RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | - |
Fragilariopsis cylindrus | RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | - |
Porosira glacialis | RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | - |
Porosira glacialis CCMP651 | RBr + 2 H2O | - |
? | |
| RH + Br- + H2O2 + H+ | - |
Fragilariopsis cylindrus CCMP3323 | RBr + 2 H2O | - |
? | |
| thymolsulfonphthalein + HBr + H2O2 | - |
Corallina officinalis | ? + 2 H2O | - |
? | |
| [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+ | - |
Fragilariopsis cylindrus | ? + 2 H2O | - |
? | |
| [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+ | - |
Porosira glacialis | ? + 2 H2O | - |
? | |
| [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+ | 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 | Corallina officinalis | ? + 2 H2O | - |
? | |
| [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+ | - |
Porosira glacialis CCMP651 | ? + 2 H2O | - |
? | |
| [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+ | - |
Fragilariopsis cylindrus CCMP3323 | ? + 2 H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bromoperoxidase | - |
Corallina officinalis |
| bromoperoxidase | - |
Fragilariopsis cylindrus |
| bromoperoxidase | - |
Porosira glacialis |
| BrPO | - |
Corallina officinalis |
| BrPO | - |
Fragilariopsis cylindrus |
| BrPO | - |
Porosira glacialis |
| V-BrPO | - |
Corallina officinalis |
| V-BrPO | - |
Fragilariopsis cylindrus |
| V-BrPO | - |
Porosira glacialis |
| vanadium-bromoperoxidase | - |
Corallina officinalis |
| vanadium-bromoperoxidase | - |
Fragilariopsis cylindrus |
| vanadium-bromoperoxidase | - |
Porosira glacialis |
| vanadium-dependent bromoperoxidase | - |
Corallina officinalis |
| vanadium-dependent bromoperoxidase | - |
Fragilariopsis cylindrus |
| vanadium-dependent bromoperoxidase | - |
Porosira glacialis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Corallina officinalis |
| 25 | - |
assay at | Fragilariopsis cylindrus |
| 25 | - |
assay at | Porosira glacialis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 5 | 60 | activity range | Corallina officinalis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.4 | - |
assay at | Fragilariopsis cylindrus |
| 6.4 | - |
assay at | Porosira glacialis |
| 7 | - |
MES buffer | Corallina officinalis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.8 | 7.8 | activity range | Corallina officinalis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| vanadate cofactor | - |
Fragilariopsis cylindrus | |
| vanadate cofactor | - |
Porosira glacialis | |
| vanadate cofactor | in the assay mixture, 2 mM/l sodium orthovanadate is added to the enzyme to ensure full loading of the active sites with vanadate | Corallina officinalis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Corallina officinalis |
| 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 | Fragilariopsis cylindrus |
| 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 | Porosira glacialis |
| additional information | fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein | Corallina officinalis |
| additional information | 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 | Fragilariopsis cylindrus |
| additional information | 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 | Porosira glacialis |
| 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 | Corallina officinalis |
| physiological function | 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 | Fragilariopsis cylindrus |
| physiological function | 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 | Porosira glacialis |
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