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Enzyme Nomenclature
Information on EC 1.11.1.18 - bromide peroxidase
for references in articles please use BRENDA:EC1.11.1.18
Word Map on EC 1.11.1.18
- 1.11.1.18
-
bromination
- nodosum
- ascophyllum
- chloroperoxidase
-
halogen
- corallina
- aureofaciens
- halide
-
curvularia
- pilulifera
- inaequalis
-
vbpos
- monochlorodimedone
- catalases
- pyrrocinia
- fucus
-
alpha/beta-hydrolase
-
rhodophyta
- synthesis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.11.1.18
-
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RECOMMENDED NAME
GeneOntology No.
bromide peroxidase
-
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the activity increased during winter and spring and peaked in late spring
-
-
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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
-
-
?
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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INHIBITORS
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
-
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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
9.9
-
crude extract, pH and temperature not specified in the publication
310
-
after 27fold purification, 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
-
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-)
4.5
-
nonhaem-type bromoperoxidase BPO 1a; nonhaem-type bromoperoxidase BPO3, at low concentrations of H2O2 (1.6 mM) the pH-optimum shifts from pH 4.5 to pH 4.0
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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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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
the enzyme is actively expressed in filamentous sporophytes
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
64000
65000
90000
90000
-
gel filtration, nonhaem-type bromoperoxidase BPO 1b; gel filtration, nonhaem-type bromoperoxidase BPO 3
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
trimer
dimer
-
2 * 3400, SDS-PAGE, nonhaem-type bromoperoxidase BPO 1a; 2 * 43000, SDS-PAGE, nonhaem-type bromoperoxidase BPO 1b
dimer
-
2 * 3400, SDS-PAGE, nonhaem-type bromoperoxidase BPO 1a; 2 * 43000, SDS-PAGE, nonhaem-type bromoperoxidase BPO 1b
-
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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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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
60
-
50 min, complete inactivation, nonhaem-type bromoperoxidase BPO 1a; 50 min, no loss of activity, nonhaem-type bromoperoxidase BPO 1b; 50 min, no loss of activity, nonhaem-type bromoperoxidase BPO 3
70
-
4 h, 36% loss of activity, BPO 2; 4 h, no inactivation of BPO 1
80
-
5 min, 50% loss of ativity, BPO 2; 5 min, no inactivation of BPO 1
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
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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
-
nonhaem-type bromoperoxidase BPO1a; nonhaem-type bromoperoxidase BPO1b; nonhaem-type bromoperoxidase BPO3
-
phenyl Sepharose column chromatography and Phenyl Sepharose 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
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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ENGINEERING
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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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.11.1.18)
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