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Information on EC 1.11.1.18 - bromide peroxidase and Organism(s) Corallina officinalis and UniProt Accession Q8LLW7
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1.11.1.18 bromide peroxidaseIUBMB Comments
Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. They catalyse the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. Bromoperoxidases also oxidize iodides.
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Word Map
- 1.11.1.18
-
bromination
- chloroperoxidase
- nodosum
- ascophyllum
-
corallina
- aureofaciens
- halide
- pilulifera
-
curvularia
- monochlorodimedone
- inaequalis
-
vbpos
- pyrrocinia
-
caldariomyces
- fumago
-
alpha/beta-hydrolase
- fucus
- synthesis
The taxonomic range for the selected organisms is: Corallina officinalis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
v-brpo, perhydrolase, bpo-a1, vanadium-dependent bromoperoxidase, bromoperoxidase ii, bromoperoxidase-catalase, bpo-a2, vanadium-containing bromoperoxidase, vbrpo, non-heme haloperoxidases, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
rVBPO
-
enzyme which is expressed by Escherichia coli as inclusion bodies and subsequently refolded
SYSTEMATIC NAME
IUBMB Comments
bromide:hydrogen-peroxide oxidoreductase
Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. They catalyse the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. Bromoperoxidases also oxidize iodides.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
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
-
?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
-
-
-
?
[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
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
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
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-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Vanadium
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetonitrile
-
sVBPO showed an increase in activity in the presence of acetonitrile, which is not observed with nVBPO or rVBPO
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
310
-
after 27fold purification, pH and temperature not specified in the publication
9.9
-
crude extract, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
optimal bromoperoxidase activity of recombinant wild-type enzyme using low substrate concentrations (0.5 mM H2O2, 5 mM Br-) and high substrate concentrations (5 mM H2O2, 100 mM Br-)
6 - 6.5
maximum bromoperoxidase activity of mutant H480A under conditions of high substrate concentrations (5 mM H2O2 and 100 mM Br-), however with reduced specific activity as compared to recombinant wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
pH 5.0: about 35% of maximal activity, pH 7.0: about 25% of maximal activity
5.5 - 10
-
pH 5.5: 70-90% of maximal activity depending on enzyme form, pH 10.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
fluorescent detection of bromoperoxidase activity in microalgae and planktonic microbial communities using aminophenyl fluorescein
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRXV_COROI
598
0
65459
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystals exhibit a teardrop morphology and are grown from 2 M ammonium dihydrogen phosphate pH and diffract to beyond 1.7 A resolution. They are in tetragonal space group P4222 with unit-cell dimensions of a = b = 201.9 A, c = 178.19 A, alpha = beta = gamma = 90°
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H480A
results in the loss of the ability to efficiently oxidize bromide, but retains the ability to oxidize iodide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
60
-
the oligomeric structure of the enzyme is not apparently disrupted by exposure to 60°C. The purified bromoperoxidase at 135 nM is maintained in the absence of any protective reagent at 60°C for 24 h. Within 30 min about 60% of the original activity is lost but no further decline in activity is seen over the full course of the incubation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolation of three forms of CoVBPO: nVBPO which is isolated directly from the algal species, sVBPO which is produced in a soluble form by Escherichia coli and rVBPO which is expressed by Escherichia coli as inclusion bodies and subsequently refolded
-
Na3VO4 is added to the crude extract (1.12 mg protein/ml) followed by heat treatment at 70°C for 2 h, 30-55% (w/v) ammonium sulfate precipitation and DEAE-52column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli. The enzyme is found to be predominantly in the form of inclusion bodies
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
Butler, A.
Vanadium haloperoxidases
Curr. Opin. Chem. Biol.
2
279-285
1998
Corallina officinalis, Ascophyllum nodosum
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)
Coupe, E.E.; Smyth, M.G.; Fosberry, A.P.; Hall, R.M.; Littlechild, J.A.
The dodecameric vanadium-dependent haloperoxidase from the marine algae Corallina officinalis: Cloning, expression, and refolding of the recombinant enzyme
Protein Expr. Purif.
52
265-272
2007
Corallina officinalis
Zhang, B.; Cao, X.; Cheng, X.; Wu, P.; Xiao, T.; Zhang, W.
Efficient purification with high recovery of vanadium bromoperoxidase from Corallina officinalis
Biotechnol. Lett.
33
545-548
2011
Corallina officinalis
Arnoldsson, K.; Andersson, P.; Haglund, P.
Formation of environmentally relevant brominated dioxins from 2,4,6,-tribromophenol via bromoperoxidase-catalyzed dimerization
Environ. Sci. Technol.
46
7239-7244
2012
Corallina officinalis (Q8LLW7)
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
Front. Mar. Sci.
6
68
2019
Corallina officinalis (Q8LLW7), Fragilariopsis cylindrus, Fragilariopsis cylindrus CCMP3323, Porosira glacialis, Porosira glacialis CCMP651
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