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EC Tree
The enzyme appears in viruses and cellular organisms
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RH + HBr + H2O2 = RBr + 2 H2O
Brings about the bromination of a range of organic molecules, forming stable C-Br bonds. Contains heme.
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bromide:hydrogen-peroxide oxidoreductase (heme-containing)
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Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
Br- + H2O2 + 3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole
2-bromo-3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole + ?
Br- + H2O2 + dianisidine
?
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Br- + H2O2 + monochlorodimedone
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additional information
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Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
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i.e. monochlorodimedone
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?
Br- + H2O2 + 3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole
2-bromo-3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole + ?
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?
Br- + H2O2 + 3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole
2-bromo-3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole + ?
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Br- + H2O2 + monochlorodimedone
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Br- + H2O2 + monochlorodimedone
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additional information
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the enzyme also shows catalase activity
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additional information
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cannot catalyze chlorination
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additional information
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in absence or presence of bromide, the enzyme is able to catalyze the oxidation of o-dianisidine, pyrogallol and o-phenylendiamine. The enzyme ahows catalase activity
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additional information
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cannot catalyze chlorination
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additional information
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in absence or presence of bromide, the enzyme is able to catalyze the oxidation of o-dianisidine, pyrogallol and o-phenylendiamine. The enzyme ahows catalase activity
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heme
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contains 0.91 molecules of heme per dimer, hame type IX
heme
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presence of a protophorphyrin IX heme group
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azide
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75 mM, 50% inhibition
cyanide
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0.023 mM, 50% inhibition
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5
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bromoperoxidase activity
5
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bromoperoxidase activity
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5 - 7
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totally inactive at pGH 4.5, pH optimum at pH 5.0, 30% of maximal activity at pH 7.0
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4
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isoelectric focusing, pH-range 3.5-9.5
4.7
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isoelectric focusing, pH-range 2.5-6.5
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EF group 70B
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brenda
NRRL B-3559
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brenda
RRL B-3559
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brenda
NRRL B-3559
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brenda
RRL B-3559
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brenda
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72500
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2 * 72500, SDS-PAGE under denaturing and non-denaturing conditions
77000
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2 * 77000, SDS-PAGE
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dimer
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2 * 77000, SDS-PAGE
dimer
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2 * 72500, SDS-PAGE under denaturing and non-denaturing conditions
dimer
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2 * 72500, SDS-PAGE under denaturing and non-denaturing conditions
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4 - 12
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30 min, stable
673375
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Kuusk, H.; Bjorklund, M.; Rydstrom, J.
Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water
Enzyme Microb. Technol.
28
617-624
2001
Pseudomonas sp.
brenda
van Pee, K.H.; Lingens, F.
Detection of a bromoperoxidase in Streptomyces phaeochromogenes
FEBS Lett.
173
5-8
1984
Streptomyces phaeochromogenes, Streptomyces phaeochromogenes NRRL B-3559
brenda
van Pee, K.H.; Lingens, F.
Purification and molecular and catalytic properties of bromoperoxidase from Streptomyces phaeochromogenes
J. Gen. Microbiol.
131
1911-1916
1985
Streptomyces phaeochromogenes, Streptomyces phaeochromogenes RRL B-3559
brenda
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