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Information on EC 1.11.1.18 - bromide peroxidase and Organism(s) Kitasatospora aureofaciens and UniProt Accession P29715
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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: Kitasatospora aureofaciens
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, v-bpo, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BPO-A1
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 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0
-
-
?
additional information
?
-
positional specificity of oxidative hydroxybromination for olefins, using rBPO-A1 and PA in the presence of methanol, is higher compared to a non-enzymatic reaction using peracetic acid. The oxidative bromination step, occurring after the enzymatic peroxidation step, is suggested to be pseudoenzymatic. Non-enzymatic oxidative bromination's influence can be disregarded under acidic condition of pH 6.0 or lower because generation of a strongly brominating active species is not the rate-limiting step under acidic conditions
-
-
-
additional information
?
-
-
positional specificity of oxidative hydroxybromination for olefins, using rBPO-A1 and PA in the presence of methanol, is higher compared to a non-enzymatic reaction using peracetic acid. The oxidative bromination step, occurring after the enzymatic peroxidation step, is suggested to be pseudoenzymatic. Non-enzymatic oxidative bromination's influence can be disregarded under acidic condition of pH 6.0 or lower because generation of a strongly brominating active species is not the rate-limiting step under acidic conditions
-
-
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by azide or cyanide. Excess bromide or chloride has no effect on its brominating activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
propanoic acid
acts as a cofactor, it has a high Log D at pH 5.0. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-
additional information
the carboxylic acids including hydroxyacetic acid, cyanoacetic acid, bromoacetic acid, chloroacetic acid, dichloroacetic acid, trichloroacetic acid, succinic acid, and malic acid, and amino acids, such as glycine, aspartic acid, glutamic acid, histidine, lysine, and arginine, are inactive as cofactors
-
additional information
-
the carboxylic acids including hydroxyacetic acid, cyanoacetic acid, bromoacetic acid, chloroacetic acid, dichloroacetic acid, trichloroacetic acid, succinic acid, and malic acid, and amino acids, such as glycine, aspartic acid, glutamic acid, histidine, lysine, and arginine, are inactive as cofactors
-
additional information
the oxidative brominating activity of an organic solvent-tolerant recombinant metal-free bromoperoxidase C-terminally tagged BPO-A1 (rBPO-A1) from Streptomyces aureofaciens depends on various additives. These include carboxylic acids, used as cofactors, and alcohols, used as water-miscible organic solvents. Propanoic acid, 2-methylpropanoic acid, and 1-butanoic acid enhanced rBPO-A1's activity by 13.7, 8.0, and 4.6fold, respectively, compared to that obtained with acetic acid. The decrease in the activity associated with changes from primary to tertiary fatty chains can be attributed to increased steric hindrance. Carboxylic acid binding structure analysis, overview
-
additional information
-
the oxidative brominating activity of an organic solvent-tolerant recombinant metal-free bromoperoxidase C-terminally tagged BPO-A1 (rBPO-A1) from Streptomyces aureofaciens depends on various additives. These include carboxylic acids, used as cofactors, and alcohols, used as water-miscible organic solvents. Propanoic acid, 2-methylpropanoic acid, and 1-butanoic acid enhanced rBPO-A1's activity by 13.7, 8.0, and 4.6fold, respectively, compared to that obtained with acetic acid. The decrease in the activity associated with changes from primary to tertiary fatty chains can be attributed to increased steric hindrance. Carboxylic acid binding structure analysis, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
145.8
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of 2-methylpropanoic acid
18.1
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of acetic acid
2.6
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of 1-butanoic acid
248.6
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of propanoic acid
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 80
reaction activity in the presence of recombinant BPO-A1 peaks at 60°C whereas peak in the non-enzymatic activity of H2O2 is not observed in temperature range of 10-70°C. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-. The active species is heat-labile. The significant decrease in activity around 65-70°C is attributed to decomposition of the active species
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
65000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 80
reaction activity in the presence of recombinant BPO-A1 peaks at 60°C whereas peak in the non-enzymatic activity of H2O2 is not observed in temperature range of 10-70°C. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-. The active species is heat-labile. The significant decrease in activity around 65-70°C is attributed to decomposition of the active species. The native BPO-A1 possesses high stability up to 80°C. Recombinant BPO-A1 possesses high peroxidating activity at high temperatures
70
80
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombiant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by ammonium sulfate fractionation and nickel affinity chromatography followed by desalting gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is overproduced in Streptomyces lividans TK64, up to 30000 times compared to Streptomyces aureofaciens
gene bpo-A1, recombiant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
China, H.; Ogino, H.
A useful propionate cofactor enhancing activity for organic solvent-tolerant recombinant metal-free bromoperoxidase (perhydrolase) from Streptomyces aureofaciens
Biochem. Biophys. Res. Commun.
516
327-332
2019
Kitasatospora aureofaciens (P33912), Kitasatospora aureofaciens, Kitasatospora aureofaciens ATCC 10762 (P33912)
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