1.11.1.B2: chloride peroxidase (vanadium-containing)
This is an abbreviated version!
For detailed information about chloride peroxidase (vanadium-containing), go to the full flat file.
Word Map on EC 1.11.1.B2
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1.11.1.B2
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inaequalis
-
curvularia
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vanadate
-
halide
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bromoperoxidase
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chlorination
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vhpos
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meroterpenoids
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glucose-6-phosphatase
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nodosum
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ascophyllum
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corallina
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prenyltransferase
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peroxo
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vanadiumv
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bipyramidal
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seaweeds
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td-dft
-
diagnostics
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synthesis
- 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
Reaction
Synonyms
chloroperoxidase, CPO, Mcl24, More, NapH1, PPHY, V-containing-haloperoxidase, vanadium chloroperoxidase, vanadium haloperoxidase, vanadium-containing chloroperoxidase, vanadium-containing peroxidase, vanadium-dependent chloroperoxidase, vanadium-dependent haloperoxidase, vCPO, VHPO
ECTree
1.11.1.B2 chloride peroxidase (vanadium-containing)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.11.1.B2 - chloride peroxidase (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
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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
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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
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chlorination in the pyrrole ring
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?
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
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chlorination in the pyrrole ring
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?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
-
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
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enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
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-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone, brominating activity of chloroperoxidase
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-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
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no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
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no activity
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-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
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no activity
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-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
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no activity
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-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
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no activity
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-
?
monochlorodimedone + Br- + H2O2
?
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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
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-
?
monochlorodimedone + Br- + H2O2
?
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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
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-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
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-
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
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?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
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-
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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
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?
additional information
?
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no peroxidase activity, no catalase activity
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-
?
additional information
?
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oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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-
?
additional information
?
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oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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?
additional information
?
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repression by addition of glucose
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?
additional information
?
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the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
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?
additional information
?
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the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase shows bactericidal and virucidal activity
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?
additional information
?
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catalytic cycle and function of the vanadium atom in the reaction mechanism, computational study using large cluster model complexes, possible pathways, and active-site protonation states, overview
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additional information
?
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vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide ions
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additional information
?
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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
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?
additional information
?
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the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
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?
additional information
?
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no substrates: geraniol and nerolidol or substrate analogues closely resembling the physiological substrate pre-merochlorin
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?
additional information
?
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VCPO Mcl24 from the merochlorin biosynthetic pathway shows an incredible ability to multitask, displaying all aforementioned VCPO function-alities (oxidative halogenation, terpene cyclization, and alpha-hydroxyketone rearrangement) within one enzyme. At pH 6.0, Mcl24 catalyzes the halogenation, oxidative dearomatization, and terpene cyclization of premerochlorin to generate two dominant monochlorinated merochlorins. These structurally divergent molecules arise due to the final terpene cyclization cascade ending with a carbon-carbon bond, or oxygen-carbon bond in merochlorins A and B, respectively. Under basic conditions (pH 8.0) the product distribution of Mcl24 is altered to predominantly catalyze the formation of merochlorin X, an alpha-hydroxyketone rearranged intermediate that may be further tailored by additional biosynthetic enzymes to generate merochlorins C and D. The major mechanistic difference during the biosyntheses of these molecules involves the addition of water to the oxidatively dearomatized molecule, which Mcl24 catalyzes more favorably at a basic pH. Hydration of the benzylic cation facilitates dichlorination and the corresponding rearrangement. in vitro, Mcl24 generates a large number of by-products because of the substantial oxidative instability of the premerochlorin substrate
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additional information
?
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in the napyradiomycin suite of molecules, VCPO NapH1 catalyzes the chloronium-induced cyclization of the dimethylallyl (prenyl) side chain of naphthomevalin to generate the tricyclic compound napyradiomycin A1, e.g. coverting methylated naphthomevalin analogue SF2415B1 isolated from Streptomyces aculeolatus NRRL 18442 to 7-methyl-napyradiomycin A1 (SF2415B3). Incubation of NapH1 with SF2415B1 in the presence of bromide facilitated a product consistent with bromonium-induced cyclization, which is a naturally produced napyradiomycin analogue. NapH1 halogenation is diastereoselective at the newly formed stereocenter at the chlorine atom, implying a specific facial chloronium formation and cyclization by the adjacent hydroxy group. NapH1 also catalyzes analogous chlorination and cyclization reactions on the des-methylated SF2415B1 substrate naphthomevalin. But NapH1 fails to show any catalytic activity on the linear terpene alcohol precursor ()-nerolidol or the related meroterpenoid-like compound lapachol, highlighting the extreme selectivity NapH1 has for its requisite substrate. Reactions catalyzed by NapH1 are also stereoselective, evidenced by the single enantiomer of napyradiomycin A1 generated from the synthetic, racemic naphthomevalin substrate. The concomitant, unreacted naphthomevalin recovered from a NapH1 assay, shows an opposite circular dichroism spectrum to naphthomevalin naturally isolated from Streptomyces bacteria or that produced in vitro by NapH3 reaction
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additional information
?
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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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?
