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Information on EC 1.11.1.18 - bromide peroxidase
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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
-
halogen
- aureofaciens
- corallina
- halide
- inaequalis
-
curvularia
- pilulifera
- monochlorodimedone
-
vbpos
- fumago
- pyrrocinia
-
alpha/beta-hydrolase
-
caldariomyces
- fucus
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
apobromoperoxidase I, BPO, BPO 1, BPO 2, BPO I, BPO-A1, BPO-A2, BPO1, bromoperoxidase, bromoperoxidase A2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BPO
BPO1
bromoperoxidase
BrPO
nonhaem-type bromoperoxidase BPO 1a
nonhaem-type bromoperoxidase BPO 1b
nonhaem-type bromoperoxidase BPO 3
nonheme bromoperoxidase
rVBPO
-
enzyme which is expressed by Escherichia coli as inclusion bodies and subsequently refolded
V-BPO
V-BrPO
vanadium bromoperoxidase
vanadium-dependent bromoperoxidase
vanadium-dependent bromoperoxidase 2
VBPO1
VBrPO(AnI)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + HBr + H2O2 = RBr + 2 H2O
Brings about the bromination of a range of organic molecules, forming stable C-Br bonds. Can also act on iodide ions. The enzymes of this group contain vanadium (V) bound to the active centre. Since the actual halogenating agents are the respective hypohalous acids, vanadium-containing halide peroxidases lack substrate specificity and regioselectivity.
-
-
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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.
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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 + (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
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 + 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 + monochlorodimedone
monobromo-monochlorodimedone + 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 + styrene
DL-1 -bromo-2-hydroxy-2-phenylethane + 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
-
-
-
-
?
phenol + H2O2 + Br-
4-bromophenol + 2-bromophenol + H2O
-
-
4-bromophenol + 2-bromophenol at the ratio of 4:1
-
?
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
-
-
?
additional information
?
-
-
strong brominating aactivity, weak chlorinating and iodating activities, catalyzes both benzylic and aromatic hydroxylations (e.g., of toluene and naphthalene)
-
-
?
additional information
?
-
enzyme uses hydrogen peroxide and bromide yielding molecular bromine as reagent for electrophilic hydrocarbon bromination
-
-
?
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
?
-
-
the alkyl hydroperoxides ethyl hydroperoxide, cuminyl hydroperoxide, and tert-butyl hydroperoxide do not support bromination of dioxygen formation catalyzed by V-BrPO
-
-
?
additional information
?
-
-
the natural brominated compound is dibromoacetaldehyde
-
-
?
additional information
?
-
-
the natural brominated compound is dibromoacetaldehyde
-
-
?
additional information
?
-
-
the alkyl hydroperoxides ethyl hydroperoxide, cuminyl hydroperoxide, and tert-butyl hydroperoxide do not support bromination of dioxygen formation catalyzed by V-BrPO
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the role of the enzyme is related to its activity as a catalase rather than as a halogenatingt agent
-
-
?
additional information
?
-
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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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
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
?
-
-
the natural brominated compound is dibromoacetaldehyde
-
-
?
additional information
?
-
-
the natural brominated compound is dibromoacetaldehyde
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the role of the enzyme is related to its activity as a catalase rather than as a halogenatingt agent
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme does require no additional cofactor
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
vanadate
in the solid state structure, every protein monomer binds one vanadate to the tele imidazole nitrogen of residue His486. In solutions of sodium orthovanadate, isoform apobromoperoxidase II recovers bromoperoxidase activity by one order of magnitude faster than apobromoperoxidase I
Vanadium
VO43+
Vanadium
-
presence of vanadium coordinated to oxygen/nitrogen either as vanadium(V) (in the native, native plus bromide, and native plus peroxide samples) or vanadium(IV) (in the reduced enzyme). There are structural changes at the metal site on reduction of the native enzyme, notably a lengthening of the average inner-shell distance and the presence of terminal oxygen together with histidine and oxygen-donating residues
Vanadium
-
the substrate bromide does not bind to active site vanadium but to a light atom, possibly carbon, in its vicinity
Vanadium
the holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres
Vanadium
-
requires vanadium for enzyme activity. The enzyme activity increases ca. 250% with the action of V5+ on the isolated enzyme, since more than 2/3 of the protein molecules are in the apo form. This effect of V5+ addition is inhibited in phosphate buffer, probably because phosphate and vanadate compete for the active site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
45% inhibition at 5 mM, 90% inhibition at 40 mM
potassium cyanide
-
0.05 mM, complete inhibition of bromoperoxidase-catalase activity
Sodium azide
-
0.05 mM, complete inhibition of bromoperoxidase-catalase activity
additional information
-
not inhibited by azide or cyanide. Excess bromide or chloride has no effect on its brominating activity
-
additional information
the enzyme is resistant to both pepsin and trypsin. The chelating agent EDTA has no discernible effect on the activity of rSt-Phy
-
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
1,1-dimethyl-4-chloro-3,5-cyclohexanedione
-
nonhaem-type bromoperoxidase BPO 3
0.0079
1,1-dimethyl-4-chloro-3,5-cyclohexanedione
-
nonhaem-type bromoperoxidase BPO 1a
0.49
Br-
mutant R379F, pH 7.0, temperature not specified in the publication
4.69
Br-
wild-type, pH 7.0, temperature not specified in the publication
8.32
Br-
mutant R379H, pH 7.0, temperature not specified in the publication
0.56
H2O2
mutant R379F, pH 7.0, temperature not specified in the publication
0.71
H2O2
wild-type, pH 7.0, temperature not specified in the publication
0.73
H2O2
mutant R379H, pH 7.0, temperature not specified in the publication
0.08
I-
wild-type, pH 7.0, temperature not specified in the publication
0.1
I-
mutant R379H, pH 7.0, temperature not specified in the publication
0.22
I-
mutant R379F, pH 7.0, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3
-
the pH optimum is independent of H2O2 and KBr when concentrations ranging from 5 to 100 mM
4.5
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
6.5
4.5
-
nonhaem-type bromoperoxidase BPO3, at low concentrations of H2O2 (1.6 mM) the pH-optimum shifts from pH 4.5 to pH 4.0
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-)
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 75
-
45°C: about 50% of maximal activity, 75°C: about 60% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
3.6
-
isoelectric focusing, pH-range 3.5-9.5, nonhaem-type bromoperoxidase BPO 3
4.5
4.6
-
isoelectric focusing, pH-range 3.5-9.5, nonhaem-type bromoperoxidase BPO 1a
4.7
-
isoelectric focusing, pH-range 3.5-9.5, nonhaem-type bromoperoxidase BPO 1b
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the activity increased during winter and spring and peaked in late spring
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the lowest specific bromoperoxidase activity occurs during the midexponential phase of growth and then increases steeply during the late stationary phase
brenda
additional information
the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations
brenda
the enzyme is actively expressed in filamentous sporophytes
brenda
-
the enzyme is actively expressed in filamentous sporophytes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (489 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
64000
65000
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
trimer
?
x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from ammonium sulfate solutions in a form suitable for X-ray diffraction analysis. Crystals are grown by the vapour-diffusion technique using the sitting-drop method. X-ray diffraction studies show that the crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with a = b = 114.3 and c = 276.0 A. The crystals diffract to at least 2.4 A resolution
structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A
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°
-
sitting drop vapour diffusion method, two crystal forms are obtained, one hexagonal form using ammonium phosphate as precipitant (form 1) and a second cubic vanadium bound form (form 2). The best crystals of the cubic form 2 containing vanadate are only obtained with the wild type enzyme. The optimised conditions use an initial protein concentration of 18 mg/ml in 50 mM Tris-H2SO4, 0.4 M KBr, 1 mM Na3VO4, 20% (w/v) polyethylene glycol 6000. For the wild type enzyme crystals grown in form 2, a mother liquor substituting the precipitant with 25% polyethylene glycol 400 and 25% polyethylene glycol 6000 is used
-
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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
R397W
-
the mutant shows a different behaviour on bromide binding compared to the wild type enzyme, (the bromide is missing the hydrogen-binding interaction that held it in the active site of the wild type enzyme)
R379F
increase in affinity for Br-, enables the mutant to oxidize Cl-, decrease in affinity for I-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57
-
20 min, 50% loss of activity, enzyme preincubated without metal ion
60
65
-
20 min, recombinantly expressed enzyme is stable, native enzyme is completely inactivated
70
75
-
20 min, 50% loss of activity, enzyme preincubated with 1 mM vanadate
80
92
-
20 min, 50% loss of activity, enzyme preincubated with 1 mM Ca2+ and 1 mM vanadium
additional information
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
additional information
-
vanadate increases the thermostability. Ag+ and Al3+ lower the thermostability of the enzyme when compared with the control. Mn2+, Fe2+, Co2+, Ni2+, and Ba2+ have slightly positive effects, whereas Li+, Na+, K+, and Rb+ have no effect and Zn2+ lowers the thermostability
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity half-life times increase along the series of buffers: phosphate
-
after treatment with a mixture of chloroform/ethanol the enzyme still shows 65% of its initial brominating activity
-
Ca2+ significantly increased the enzyme stability. Strontium and magnesium ions have similar effects
-
circular dichroism measurements showed that the secondary structure is not affected upon incubation in 4% SDS
-
denaturation did not occur upon incubation in 4 M guanidine hydrochloride
-
dialysis of the enzyme preparation against 1 mM EDTA in 0.1 M citrate-phosphate buffer (pH 3.8) results in loss of enzymic activity. Incubation with vanadium, does not restore the enzymic activity. Also various other metal ions: Zn(II), Fe(II), Cu(II) and Mn(II) are ineffective in the reactivation of the preparation
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-propanol
-
completely intact in the presence of 50% methanol
Methanol
-
completely intact in the presence of 50% methanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, in 0.001 mM H2O2-incubated, MES-buffered (pH 6.22) aqueous alcoholic solution, half-life time of about 60 days
-
20°C, in 0.001 mM NaCl-incubated, MES-buffered (pH 6.22) aqueous alcoholic solution, half-life time of about 24 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Ni-NTA column chromatography, and DE52 gel filtration
-
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
-
phenyl Sepharose column chromatography and Phenyl Sepharose gel filtration
-
recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is overproduced in Streptomyces lividans TK64, up to 30000 times compared to Streptomyces aureofaciens
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli. Recombinant enzyme and its mutants have no enzyme activities, unless they are activated by Na3VO4
gene phyA, DNA and amino acid sequence determination and analysis, recombinant expression of the codon-optimized phytase gene in Pichia pastoris strain X-33, quantitative real-time PCR for gene copy number determination
overexpressed in Escherichia coli. The enzyme is found to be predominantly in the form of inclusion bodies
-
the gene is cloned in the positive selection vector pIJ699 and expression in Streptomyces lividans TK64. The cloned bromoperoxidase is overproduced up to 2800fold by the Streptomyces lividans transformant
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is repressed in gametophytes throughout growth period
transcript abundance is relatively higher in seaweed samples treated with 50 parts per thousand artificial seawater compared to those treated in 10 and 30 parts per thousand artificial seawater
the enzyme is repressed in gametophytes throughout growth period
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
immobilization of enzyme on magnetic micrometre-sized particles in quantitative yields, with up to 40% retention of initial bromoperoxidase activity. The immobilized enzyme is stable with a half-life time of about 160 days. It serves as reusable catalyst for bromide oxidation with H2O2 in up to 14 consecutive experiments. Immobilized enzyme is used for methyl pyrrole-2-carboxylate conversion into derivatives of naturally occurring compounds e.g. from Agelas oroides with product selectivity of up to 75%
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REF.
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TITLE
JOURNAL
VOL.
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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
brenda
Hofrichter, M.; Ullrich, R.
Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance
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71
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2006
Agrocybe aegerita
brenda
Itoh, N.; Morinaga, N.; Kouzai, T.
Oxidation of aniline to nitrobenzene by nonheme bromoperoxidase
Biochem. Mol. Biol. Int.
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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
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284S
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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
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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
J. Gen. Microbiol.
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
J. Gen. Microbiol.
138
1123-1131
1992
Kitasatospora aureofaciens (P29715), Kitasatospora aureofaciens
brenda
Hara, I.; Sakurai, T.
Isolation and characterization of vanadium bromoperoxidase from a marine macroalga, Ecklonia stolonifera
J. Inorg. Biochem.
72
23-28
1998
Ecklonia cava subsp. stolonifera
brenda
Rehder, D.; Schulzke, C.; Dau, H.; Meinke, C.; Hanss, J.; Epple, M.
Water and bromide in the active center of vanadate-dependent haloperoxidases
J. Inorg. Biochem.
80
115-121
2000
Ascophyllum nodosum
brenda
Carter, J.N.; Beatty, K.E.; Simpson, M.T.; Butler, A.
Reactivity of recombinant and mutant vanadium bromoperoxidase from the red alga Corallina officinalis
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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
140
509-516
1994
Kitasatospora aureofaciens
brenda
Facey, S.J.; Gross, F.; Vining, L.C.; Yang, K.; van Pee, K.H.
Cloning, sequencing and disruption of a bromoperoxidase-catalase gene in Streptomyces venezuelae: evidence that it is not required for chlorination in chloramphenicol biosynthesis
Microbiology
142
657-665
1996
Streptomyces venezuelae
brenda
Almeida, M.; Filipe, S.; Humanes, M.; Maia, M.F.; Melo, R.; Severino, N.; da Silva, J.A.; Frausto da Silva, J.J.; Wever, R.
Vanadium haloperoxidases from brown algae of the Laminariaceae family
Phytochemistry
57
633-642
2001
Saccharina latissima, Laminaria hyperborea
brenda
Ohsawa, N.; Ogata, Y.; Okada, N.; Itoh, N.
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
58
683-692
2001
Corallina pilulifera
brenda
Ohshiro, T.; Hemrika, W.; Aibara, T.; Wever, R.; Izumi, Y.
Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the recombinant enzyme
Phytochemistry
60
595-601
2002
Corallina pilulifera
brenda
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
brenda
Kamenarska, Z.; Taniguchi, T.; Ohsawa, N.; Hiraoka, M.; Itoh, N.
A vanadium-dependent bromoperoxidase in the marine red alga Kappaphycus alvarezii (Doty) Doty displays clear substrate specificity
Phytochemistry
68
1358-1366
2007
Kappaphycus alvarezii, Kappaphycus alvarezii Doty
brenda
Littlechild, J.; Garcia Rodriguez, E.; Isupov, M.
Vanadium containing bromoperoxidase--insights into the enzymatic mechanism using X-ray crystallography
J. Inorg. Biochem.
103
617-621
2009
Corallina pilulifera
brenda
Waller, M.P.; Geethalakshmi, K.R.; Buehl, M.
51V NMR chemical shifts from quantum-mechanical/molecular-mechanical models of vanadium bromoperoxidase
J. Phys. Chem. B
112
5813-5823
2008
Ascophyllum nodosum (P81701)
brenda
Geethalakshmi, K.R.; Waller, M.P.; Thiel, W.; Buehl, M.
51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases
J. Phys. Chem. B
113
4456-4465
2009
Ascophyllum nodosum (P81701)
brenda
Hartung, J.; Bruecher, O.; Hach, D.; Schulz, H.; Vilter, H.; Ruick, G.
Bromoperoxidase activity and vanadium level of the brown alga Ascophyllum nodosum
Phytochemistry
69
2826-2830
2008
Ascophyllum nodosum
brenda
Hartung, J.; Dumont, Y.; Greb, M.; Hach, D.; Koehler, F.; Schulz, H.; Casny, M.; Rehder, D.; Vilter, H.
On the reactivity of bromoperoxidase I (Ascophyllum nodosum) in buffered organic media: Formation of carbon bromine bonds
Pure Appl. Chem.
81
1251-1264
2009
Ascophyllum nodosum
-
brenda
Chen, B.; Cai, Z.; Wu, W.; Huang, Y.; Pleiss, J.; Lin, Z.
Morphing activity between structurally similar enzymes: From heme-free bromoperoxidase to lipase
Biochemistry
48
11496-11504
2009
Kitasatospora aureofaciens (P29715), Kitasatospora aureofaciens
brenda
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
brenda
Sandy, M.; Carter-Franklin, J.N.; Martin, J.D.; Butler, A.
Vanadium bromoperoxidase from Delisea pulchra: enzyme-catalyzed formation of bromofuranone and attendant disruption of quorum sensing
Chem. Commun. (Camb. )
47
12086-12088
2011
Delisea pulchra
brenda
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)
brenda
Wischang, D.; Hartung, J.; Hahn, T.; Ulber, R.; Stumpf, T.; Fecher-Trost, C.
Vanadate(v)-dependent bromoperoxidase immobilized on magnetic beads as reusable catalyst for oxidative bromination
Green Chem.
13
102-108
2011
Ascophyllum nodosum (P81701)
-
brenda
Johnson, T.; Palenik, B.; Brahamsha, B.
Characterization of a functional vanadium-dependent bromoperoxidase in the marine cyanobacterium synechococcus SP. CC9311
J. Phycol.
47
792-801
2011
Synechococcus sp., Synechococcus sp. (Q0I6Q3), Synechococcus sp. WH8020, Synechococcus sp. CC9311 (Q0I6Q3)
brenda
Baharum, H.; Chu, W.C.; Teo, S.S.; Ng, K.Y.; Rahim, R.A.; Ho, C.L.
Molecular cloning, homology modeling and site-directed mutagenesis of vanadium-dependent bromoperoxidase (GcVBPO1) from Gracilaria changii (Rhodophyta)
Phytochemistry
92
49-59
2013
Gracilaria changii (L7YCT6), Gracilaria changii
brenda
Wischang, D.; Hartung, J.
Bromination of phenols in bromoperoxidase-catalyzed oxidations
Tetrahedron
68
9456-9463
2012
Ascophyllum nodosum (P81701)
-
brenda
Weyand, M.; Hecht, H.J.; Vilter, H.; Schomburg, D.
Crystallization and preliminary X-ray analysis of a vanadium-dependent peroxidase from Ascophyllum nodosum
Acta Crystallogr. Sect. D
52
864-865
1996
Ascophyllum nodosum (P81701), Ascophyllum nodosum
brenda
Weyand, M.; Hecht, H.; Kiess, M.; Liaud, M.; Vilter, H.; Schomburg, D.
X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution
J. Mol. Biol.
293
595-611
1999
Ascophyllum nodosum (P81701), Ascophyllum nodosum
brenda
Kaneko, K.; Washio, K.; Umezawa, T.; Matsuda, F.; Morikawa, M.; Okino, T.
cDNA cloning and characterization of vanadium-dependent bromoperoxidases from the red alga Laurencia nipponica
Biosci. Biotechnol. Biochem.
78
1310-1319
2014
Laurencia nipponica
brenda
Matsuda, R.; Ozgur, R.; Higashi, Y.; Takechi, K.; Takano, H.; Takio, S.
Preferential expression of a bromoperoxidase in sporophytes of a red alga, Pyropia yezoensis
Mar. Biotechnol.
17
199-210
2015
Pyropia yezoensis (A0A0A8J7X1), Pyropia yezoensis TU-1 (A0A0A8J7X1)
brenda
Ranjan, B.; Satyanarayana, T.
Recombinant HAP phytase of the thermophilic mold Sporotrichum thermophile expression of the codon-optimized phytase gene in Pichia pastoris and applications
Mol. Biotechnol.
58
137-147
2016
Thermothelomyces thermophilus (V5M269)
brenda
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