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Information on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing)
for references in articles please use BRENDA:EC1.11.1.B2preliminary BRENDA-supplied EC number
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EC Tree
1.11.1.B2 chloride peroxidase (vanadium-containing)Specify your search results
Word Map
- 1.11.1.B2
- inaequalis
-
curvularia
- vanadate
- halide
-
bromoperoxidase
-
chlorination
-
vhpos
-
meroterpenoids
- glucose-6-phosphatase
- nodosum
-
ascophyllum
-
corallina
- prenyltransferase
-
peroxo
-
vanadiumv
-
bipyramidal
- seaweeds
-
td-dft
- diagnostics
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
vanadium chloroperoxidase, vanadium-dependent haloperoxidase, vanadium-containing chloroperoxidase, naph1, vanadium-dependent chloroperoxidases, mcl24, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPO
NapH1
vanadium chloroperoxidase
vanadium-dependent chloroperoxidases
vanadium-dependent haloperoxidase
vCPO
-
vanadium chloroperoxidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
-
-
-
-
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
Curvularia inaequalis
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
chloride:hydrogen-peroxide oxidoreductase (vanadium-containing)
-
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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
1,1-dimethyl-4-chloro-3,5-cyclohexanedione + Cl- + H2O
?
-
-
-
?
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
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+
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+
Cl- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
methyl p-tolyl sulfide + H2O2
p-tolyl methyl sulfoxide
-
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-
-
-
?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
-
-
-
?
monochlorodimedone + bromide + H2O2 + H+
bromochlorodimedone + 2 H2O
-
-
-
?
monochlorodimedone + chloride + H2O2 + H+
dichlorodimedone + H2O
-
-
-
?
pre-merochlorin + Cl- + H+ + H2O2
merochlorin A + merochlorin B + 2 H2O
-
-
-
?
styrene + KBr + H2O2
2-bromo-1-phenylethan-1-ol + 2-phenyloxirane + 2 H2O
-
-
-
?
styrene + KCl + H2O2
2-chloro-1-phenylethan-1-ol + 2 H2O
-
-
-
?
[(1E)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2R)-2-bromo-1-phenylpropan-1-ol + 2 H2O
-
-
-
?
[(1Z)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2S)-2-bromo-1-phenylpropan-1-ol + 2 H2O
-
-
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
-
chlorination in the pyrrole ring
-
?
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
-
chlorination in the pyrrole ring
-
?
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
-
chlorination in the pyrrole ring
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
-
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
-
?
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, brominating activity of chloroperoxidase
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedone + Br- + H2O2
?
-
all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated
-
-
?
monochlorodimedone + Br- + H2O2
?
-
all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated
-
-
?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
-
-
-
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
-
uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
-
-
uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
-
?
additional information
?
-
-
no peroxidase activity, no catalase activity
-
-
?
additional information
?
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
repression by addition of glucose
-
-
?
additional information
?
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
additional information
?
-
the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase shows bactericidal and virucidal activity
-
-
?
additional information
?
-
-
prochiral selectivity in H2O2-promoted oxidation of arylalkanols, the cleavage of the pro-S C-H bond always predominating over the cleavage of the pro-R C-H bond
-
-
?
additional information
?
-
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
additional information
?
-
no substrates: geraniol and nerolidol or substrate analogues closely resembling the physiological substrate pre-merochlorin
-
-
?
additional information
?
-
meta-vanadate and ortho-vanadate, exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with substrate phytate, molecular docking study and inhibition mechanism, overview. The active site of haloperoxidase shows close similarity with histidine acid phytases. Inhibition of phytase by vanadate can make the enzyme behave as a vanadate-dependent haloperoxidase provided phosphoesterase activity of the enzyme is shut down by the vanadate. The vanadate exists as an anion at pH 3.0 and possibly binds to the active site cleft of phytase, which has a cluster of positively charged amino acids arginine, lysine, and histidine below the isoelectric point (pI) of the enzyme. Upon molecular docking of metavanadate with the rPPHY, it was observed to interact with the same amino acid residues of the catalytic site, with which substrate interacts. Both inhibitor and substrate might sit into the catalytic cleft of the enzyme which is placed between conserved alpha/beta-domain and a variable alpha-domain of rPPHY. When bonding of the substrate/inhibitor was analyzed, it is found to form bonds with arginine (R70), arginine (R74), and aspartate (D344). Inhibition kinetics of phytase by metavanadate. Inhibition of phytase by metavanadate suggests the applicability of rPPHY as haloperoxidase. The reaction is carried out with KBr, metavanadate, H2O2, and phenol red, while observed intermittently for change in color from red-orange to blue-violet
-
-
?
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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
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
-
?
pre-merochlorin + Cl- + H+ + H2O2
merochlorin A + merochlorin B + 2 H2O
-
-
-
?
additional information
?
-
repression by addition of glucose
-
-
?
additional information
?
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
additional information
?
-
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vanadate
Vanadium
vanadate
the vanadate cofactor changes its protonation from quadruply protonated at pH 6.3 to triply protonated at pH 7.3 to doubly protonated at pH 8.3. In the mutant P395D/L241V/T343A, the vanadate protonation is the same at pH 5.0 and 8.3, and the cofactor is doubly protonated
Vanadium
the vanadate binding pocket seems to form a very rigid frame stabilizing oxyanion binding
Vanadium
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Pervanadate is bound much more strongly to the enzyme than vanadate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Br-
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
hydrazine
uncompetitive; uncompetitive inhibition, inhibition constant: 0.3 mM
hydroxylamine
competitive and uncompetitive inhibition; inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant: 0.04 mM, uncompetitive inhibition 0.08 mM
NO3-
pH 5.5: competitive inhibition of the chlorination reaction with respect to chloride, uncompetitive with respect to H2O2
azide
uncompetitive; uncompetitive inhibition, inhibition constant: 50 nM
phosphate
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Presence of H2O2 prevents inactivation by phosphate; substitution of vanadate in the active site by phosphate leads to inactivation. Presence of H2O2 prevents the inactivation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
5.5
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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5.5
pH 3.5: about 70% of maximal activity, pH 5.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
348332, 348333, 348335, 348336, 348337, 348338, 348342, 657588, 658904, 659641, 674779, 687350, 688195, 697156, 698914, 699774, 712657, 712779, 725614, 742267, 742747
UniProt
brenda
recombinantly overexpressed in Saccharomyces cerevisiae
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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