Information on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.11.1.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
chloride peroxidase (vanadium-containing)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
chloride:hydrogen-peroxide oxidoreductase (vanadium-containing)
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1-dimethyl-4-chloro-3,5-cyclohexanedione + Cl- + H2O
?
show the reaction diagram
-
-
-
-
?
3-chloro-2-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-2,5,7-trihydroxy-6-methyl-3-(3-methylbut-2-en-1-yl)-2,3-dihydronaphthalene-1,4-dione + bromide + H2O2
(3R)-3-bromo-4a-chloro-10a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-6,8-dihydroxy-2,2,7-trimethyl-3,4,4a,10a-tetrahydro-2H-benzo[g]chromene-5,10-dione + H+
show the reaction diagram
3-chloro-2-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-2,5,7-trihydroxy-6-methyl-3-(3-methylbut-2-en-1-yl)-2,3-dihydronaphthalene-1,4-dione + chloride + H2O2
(3R)-3,4a-dichloro-10a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-6,8-dihydroxy-2,2,7-trimethyl-3,4,4a,10a-tetrahydro-2H-benzo[g]chromene-5,10-dione + H+
show the reaction diagram
3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + Cl- + H2O2
monochloropyrrolnitrin + dichloropyrrolonitrin
show the reaction diagram
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
show the reaction diagram
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
show the reaction diagram
Br- + H2O2 + H+
HOBr + H2O
show the reaction diagram
-
-
-
-
?
Cl- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
show the reaction diagram
-
i.e. monochlorodimedone
-
-
?
Cl- + H2O2 + H+
HOCl + H2O
show the reaction diagram
-
-
-
-
?
I- + H2O2 + H+
HOI + H2O
show the reaction diagram
-
-
-
-
?
indole + Br- + H2O2
?
show the reaction diagram
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
show the reaction diagram
methyl p-tolyl sulfide + H2O2
p-tolyl methyl sulfoxide
show the reaction diagram
-
in absence of Cl- the oxidation is enantioselective and an oxygen atom of H2O2 is incorporated in the sulfoxide, in the presence of Cl- the oxidation is not enantioselective and there is no incorporation of oxygen from H2O2. The sulfide oxidation takes place through an enzyme-generated freely dissociable oxidized halogen intermediate formed by the interaction of enzyme-OCl- with Cl-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
show the reaction diagram
monochlorodimedone + Br- + H2O2
?
show the reaction diagram
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
show the reaction diagram
-
-
-
-
?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
show the reaction diagram
monochlorodimedone + chloride + H2O2 + H+
dichlorodimedone + H2O
show the reaction diagram
-
-
-
-
?
monochlorodimedone + Cl- + H2O2
dichlorodimedone + H2O
show the reaction diagram
-
-
-
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
show the reaction diagram
-
enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
-
?
Br- + H2O2 + H+
HOBr + H2O
show the reaction diagram
-
-
-
-
?
Cl- + H2O2 + H+
HOCl + H2O
show the reaction diagram
-
-
-
-
?
I- + H2O2 + H+
HOI + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
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enzyme contains heme
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
vanadate
Vanadium
Zinc
-
contains 0.3 mol of zinc per mol of enzyme
additional information
-
enzyme contains no metal
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
azide
Br-
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inhibition of mutant enzyme S402A between pH 3.5 and 4.5: concentrations greater than 0.2 mM inhibit, between pH 5.0 and 5.5: concentrations above 0.5 mM inhibit, between pH 6.0 and 6.3: 0.5 mM does not inhibit the mutant enzyme
Cl-
-
pH 4.1: mixed type inhibition with respect to H2O2, pH 3.1: competitive inhibition
H2O2
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above 50 mM
hydrazine
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uncompetitive; uncompetitive inhibition, inhibition constant: 0.3 mM
hydroxylamine
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competitive and uncompetitive inhibition; inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant: 0.04 mM, uncompetitive inhibition 0.08 mM
KCN
-
0.01 mM, 50% inhibition
NO3-
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pH 5.5: competitive inhibition of the chlorination reaction with respect to chloride, uncompetitive with respect to H2O2
phosphate
[Fe(CN)6]4+
-
0.7 mM, 50% inhibition of brominating activity
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[Fe(CN6)]3+
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0.82 mM, 50% inhibition of brominating activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11 - 177
Br-
0.9 - 474
Cl-
0.04 - 81.2
H2O2
additional information
additional information
-
Km-value for Cl- is pH-dependent whereas the Km-value for Br- is hardly pH-dependent
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.1 - 200
Br-
1.13 - 23
Cl-
15.2 - 183
H2O2
additional information
additional information
Curvularia inaequalis
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
hydrazine
-
-
0.04 - 0.08
hydroxylamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.24
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bromoperoxidase activity
4.23
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chloroperoxidase activity
additional information
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
4.1 - 4.9
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bromination of monochlorodimedone
4.5
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recombinant CVPO and mutant enzyme S402A
5
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chlorination of monochlorodimedone
5 - 5.5
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bromination of monochlorodimedone
5.5
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the wild type enzyme shows maximal activity at a pH of 5.5, but at pH of 7.7, its activity is decreased a 1000fold
7
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brominating activity of mutant enzyme H404A
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 5.5
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pH 3.5: about 70% of maximal activity, pH 5.5: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 67488, calculation from nucleotide sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method. High-resolution crystal structure (1.5 A resolution) of the reaction of the phosphate monoester p-nitrophenylphosphate with apo-VCPO exhibits a trapped intermediate of the phosphohydrolase reaction
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8.5
-
stable
348343
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
2 h, stable
65
-
2 h, stable
80
-
initial decrease of activity, after which the enzyme remains stable for 6.5 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-methoxyethanol, 7.5% v/v, 50% loss of activity
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ethanol, 15% v/v, 50% loss of activity
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methanol, 40% v/v, 50% loss of activity
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VCPO is active in chlorination and singlet oxygenation in non-ionic microemulsions
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme remains active 10 h corresponding to 125.000 turnover with respect to O2
-
712779
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, sodium acetate buffer, pH 5.5, stable for months
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4C, 0.1 M sodium acetate buffer, pH 3.5-5.5, 0.1 M ammonium acetate buffer, pH 6.0-7.0, 0.1 M potassium phosphate buffer, pH 7.0-8.5, stable for over 2 months
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6C, 20 mM sodium acetate buffer, pH 3.5-6, or ammonium acetate buffer, pH 6-8, stable for weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant CPO and mutant enzymes S402A and F397H are overexpressed as apoenzyme in Saccharomyces cerevisiae
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recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3000fold overexpression in Streptomyces aureofaciens T24-88
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expressed in Escherichia coli
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expressed in Saccharomyces cerevisiae
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expression in Escherichia coli
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expression in Saccharomyces cerevisiae
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recombinant CPO and mutant enzymes S402A and F397H are overexpressed as apoenzyme in Saccharomyces cerevisiae
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F397H
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12% of the activity of the wild-type enzyme (chlorination of monochlorodimedone), mutant enzyme shows enhancement of bromination activity under certain conditions, inactivation of the mutant enzyme by halide especially at low pH is observed during turnover
H496A
-
enzyme loses the ability to bind vanadate covalently, resulting in an inactive enzyme
K353A
-
,enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase, no clear pH-optimum
P395D
-
10fold increase in brominating activity at pH 8
P395D/L241V/T343A
P395E
-
10fold increase in brominating activity at pH 8
P395H/A399S
-
5fold increase in brominating activity at pH 8
P395T
-
6fold increase in brominating activity at pH 8
P395T/L241V
-
19fold increase in brominating activity at pH 8
P395T/L241V/T343A
-
20fold increase in brominating activity at pH 8
P395T/T343A
-
14fold increase in brominating activity at pH 8
R360A
-
,enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
R360C/I391V
-
5fold increase in brominating activity at pH 8
R490A
-
,enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
S402A
-
1.8% of the activity of wild-type enzyme (chlorination of monochlorodimedone), mutation decreases activity, mutant enzyme still catalyzes efficiently oxidation of both Cl- and Br-
H420F
-
inactive
S427H
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the mutant shows nearly wild type activity at approximately 70% in the monochlorodimedone assay but is unable to catalyze the conversion of 3 into 4 or 5. Instead, the mutant exclusively catalyzes the formation of 3-based bromohydrins
H420F
-
inactive
-
S427H
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the mutant shows nearly wild type activity at approximately 70% in the monochlorodimedone assay but is unable to catalyze the conversion of 3 into 4 or 5. Instead, the mutant exclusively catalyzes the formation of 3-based bromohydrins
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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the observed bactericidal and virucidal activity of the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase is an important step forward in the application of this robust enzyme as a component in disinfection formulations