Information on EC 1.11.1.10 - chloride peroxidase

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

EC NUMBER
COMMENTARY hide
1.11.1.10
-
RECOMMENDED NAME
GeneOntology No.
chloride peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RH + chloride + H2O2 = RCl + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
oxidative dehalogenation
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-
redox reaction
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reduction
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sulfoxidation
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SYSTEMATIC NAME
IUBMB Comments
chloride:hydrogen-peroxide oxidoreductase
Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.
CAS REGISTRY NUMBER
COMMENTARY hide
9055-20-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-citronellol + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
(+/-)-linalool + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
(-)-alpha-pinene + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
(-)-beta-pinene + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
(1R,2S)-(+)-2-benzylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(+)-2-benzyl-1-formylcyclopropane + ?
show the reaction diagram
-
-
-
-
?
(1R,2S)-(+)-2-ethylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-2-ethyl-1-formylcyclopropane + ?
show the reaction diagram
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-
-
-
?
(1R,2S)-(+)-2-methylcyclopropanemethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-2-methyl-1-formylcyclopropane + ?
show the reaction diagram
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-
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?
(1R,2S)-(+)-2-propylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-1-formyl-2-propylcyclopropane + ?
show the reaction diagram
-
-
-
-
?
(1R,2S)-(-)-2-acetoxymethylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-2-acetoxymethyl-1-formylcyclopropane + ?
show the reaction diagram
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-
-
-
?
(1R,2S)-cyclohexa-3,5-diene-1,2-diyl diacetate + tert-butyl hydroperoxide
(1S,2S,3S,6S)-7-oxabicyclo[4.1.0]hept-4-ene-2,3-diyl diacetate + (1R,2S,5R,6S)-5,6-dihydroxycyclohex-3-ene-1,2-diyl diacetate + ?
show the reaction diagram
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-
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?
(1S)-3-carene + Cl- + H2O2
(1S,3R,4R,6R)-4-chloro-3,7,7-trimethyl-bicyclo[4.1.0]heptane-3-ol + H2O
show the reaction diagram
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-
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?
(2E)-hex-2-en-1-ol + tert-butyl hydroperoxide
trans-(3-propyloxiran-2-yl)methanol + H2O
show the reaction diagram
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-
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?
(2Z)-hex-2-en-1-ol + tert-butyl hydroperoxide
cis-(3-propyloxiran-2-yl)methanol + H2O
show the reaction diagram
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?
(2Z)-pent-2-en-1-ol + tert-butyl hydroperoxide
cis-2-(3-ethyloxiran-2-yl)ethanol + (3Z)-hex-3-enal + H2O
show the reaction diagram
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-
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?
(3E,5E)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4E)-6-oxohepta-2,4-dienal + (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one + (2E)-4-oxopent-2-enal
show the reaction diagram
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-
83% (2E,4E)-6-oxohepta-2,4-dienal, 4% (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one, and 13% (2E)-4-oxopent-2-enal
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?
(3Z,5E)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4Z)-6-oxohepta-2,4-dienal + (2E)-4-oxopent-2-enal + (2E,4E)-6-oxohepta-2,4-dienal
show the reaction diagram
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78% (2E,4Z)-6-oxohepta-2,4-dienal, 15% (2E)-4-oxopent-2-enal and 7% (2E,4E)-6-oxohepta-2,4-dienal
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?
(3Z,5Z)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4Z)-6-oxohepta-2,4-dienal + (2E)-4-oxopent-2-enal + (3Z)-4-[(2S,3S)-3-methyloxiran-2-yl]but-3-en-2-one
show the reaction diagram
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27% (2E,4Z)-6-oxohepta-2,4-dienal, 38% (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one and 35% (3Z)-4-[(2S,3S)-3-methyloxiran-2-yl]but-3-en-2-one
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?
(4Z)-hex-4-en-1-ol + tert-butyl hydroperoxide
3-(3-methyloxiran-2-yl)propan-1-ol + (4Z)-hex-4-enal + H2O
show the reaction diagram
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-
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?
(5R,6S)-5,6-dimethoxycyclohexa-1,3-diene + tert-butyl hydroperoxide
(1S,4S,5S,6S)-4,5-dimethoxy-7-oxabicyclo[4.1.0]hept-2-ene + ?
show the reaction diagram
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?
(R)-limonene + Cl- + H2O2
?
show the reaction diagram
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?
(R)-limonene + H2O2
(1S,2S,4R)-limonene-1,2-diol + (1R,2R)-4R-limonene-1,2-diol + ?
show the reaction diagram
-
when the reaction is carried out in the presence of chloride ions an enhancement in the reaction rate is observed, maintaining the regioselectivity, but not the stereoselectivity. The reaction products under these conditions are (1S,2S)-4R-limonene-1,2-diol and (1R,2R)-4R-limonene-1,2-diol. In the presence of potassium chloride the limonene oxidation also occurs by the produced hypochlorite without stereoselectivity
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-
?
(R)-limonene + H2O2
(1S,2S,4R)-limonene-1,2-diol + H2O
show the reaction diagram
-
in the absence of chloride ions, at pH 3 or pH 6, the reaction is regio and stereoselective with a diasteromeric excess of more than 99% of (1S,2S)-4R-limonene-1,2-diol
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?
(Z)-beta-ocimene + Cl- + H2O2
?
show the reaction diagram
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-
-
?
1,2-dihydronaphthalene + tert-butyl hydroperoxide
(1R,2R)-dihydroxytetrahydronaphthalene + ?
show the reaction diagram
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?
1,3-cycloheptadiene + tert-butyl hydroperoxide
(1R,3R)-cyclohept-3-ene-1,2-diol + (1R,4S)cyclohept-2-ene-1,4-diol + (1R,4R)-cyclohept-2-ene-1,4-diol + ?
show the reaction diagram
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?
1,3-cyclooctadiene + tert-butyl hydroperoxide
cycloocta-1,4-dien-1-yl hydroperoxide + cycloocta-2,4-dien-1-ol + ?
show the reaction diagram
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-
main product is cycloocta-1,4-dien-1-yl hydroperoxide, formation of small amounts of cycloocta-2,4-dien-1-ol
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?
2 pyrene + 3 KCl + 3 H2O2
chloropyrene + dichloropyrene + 3 KOH + 3 H2O
show the reaction diagram
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-
?
2'-deoxyuridine + Br- + H2O2
5-bromo-2'-deoxyuridine + H2O
show the reaction diagram
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-
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?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + HCl
?
show the reaction diagram
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-
-
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?
2,3,5,6-tetrachloroaniline + HCl + H2O2
pentachloroaniline + H2O
show the reaction diagram
-
the main product from peroxidase oxidation is a polymeric and insoluble material
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-
?
2,3,5,6-tetrachlorophenol + Cl- + H2O2
pentachlorophenol + H2O
show the reaction diagram
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-
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?
2,3,5,6-tetrachlorophenol + HCl + H2O2
pentachlorophenol + H2O
show the reaction diagram
-
the main product from peroxidase oxidation is a polymeric and insoluble material
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-
?
2,4,6-trichlorophenol + H2O2
2,6-dichloro-1,4-benzoquinone + H2O + HCl
show the reaction diagram
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-
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-
?
2,4,6-trichlorophenol + H2O2
?
show the reaction diagram
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oxidative dehylogenation
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?
2,4-dichlorophenol + Cl- + H2O2
?
show the reaction diagram
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-
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?
2-aminophenol + H2O2
?
show the reaction diagram
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?
2-exo-methylbicyclo[2.2.1]hept-5-ene-2-endo-carboxylic acid + Br- + H2O2
corresponding delta lactone + ?
show the reaction diagram
-
-
-
?
2-methyl-4-propylcyclopentane-1,3-dione + Cl- + H2O2
2-chloro-2-methyl-4-propylcyclopentane-1,3-dione + H2O
show the reaction diagram
-
reaction without appreciable stereoselectivity
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?
2-methylanthracene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
3,4-dichloroaniline + H2O2
?
show the reaction diagram
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-
-
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?
3-aminophenol + H2O2
?
show the reaction diagram
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-
-
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?
3-anisidine + H2O2
?
show the reaction diagram
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-
-
-
?
4,6-dimethyldibenzothiophene + Cl- + H2O2
?
show the reaction diagram
-
the substrate exists as a monomeric and dimeric species in aqueous acetonitrile solutions. Oxidation of dimer substrate is preferred when compared to monomer oxidation
-
-
?
4-aminobenzoic acid + H2O2
?
show the reaction diagram
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-
-
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?
4-aminophenol + H2O2
?
show the reaction diagram
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-
-
-
?
4-anisidine + H2O2
?
show the reaction diagram
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-
-
-
?
4-chloroaniline + chloride + H2O2
?
show the reaction diagram
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-
-
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?
4-chloroaniline + H2O2
4-chloronitrosobenzene + H2O
show the reaction diagram
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-
-
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?
4-chlorophenol + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
4-chlorophenol + H2O2
?
show the reaction diagram
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-
-
-
?
4-chlorophenol + H2O2 + Cl-
?
show the reaction diagram
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-
-
-
?
4-fluorophenol + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
4-fluorophenol + H2O2
1,4-benzoquinone + ?
show the reaction diagram
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-
-
-
?
4-toluidine + H2O2
?
show the reaction diagram
-
-
-
-
?
5-hexen-1-ol + tert-butyl hydroperoxide
5-hexenal + ?
show the reaction diagram
-
-
only a small amount is produced
-
?
5-hexen-1-ol + tert-butyl hydroperoxide
hex-5-enal + H2O
show the reaction diagram
-
-
-
-
?
7,12-dimethylbenzanthracene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
7-azaindole + H2O2
7-azaoxindole + H2O
show the reaction diagram
-
cross-linked enzyme aggregates
-
-
?
7-methylbenzo[a]pyrene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
9-methylanthracene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
acenaphthene + Cl- + H2O2
dichloroacenaphthene + trichloroacenaphthene + H2O
show the reaction diagram
-
-
-
?
anthracene + 2 KCl + 2 H2O2
9,10-dichloroanthracene + 2 KOH + 2 H2O
show the reaction diagram
-
-
-
-
?
anthracene + Cl- + H2O2
9,10-dichloroanthracene + H2O
show the reaction diagram
-
-
-
?
azulene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
benzo[a]pyrene + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
benzo[ghi]perylene + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
benzyl-N-(2-hydroxyethyl)-carbamate + tertbutyl hydroperoxide
Cbz-glycinal + ?
show the reaction diagram
-
-
-
-
?
beta-myrcene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
biphenylene + Cl- + H2O2
dichlorobiphenylene + trichlorobiphenylene + H2O
show the reaction diagram
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-
-
?
Boc-D-methionine-methyl ester + H2O2
Boc-D-methionine-methyl ester sulfoxide + H2O
show the reaction diagram
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-
-
-
?
Boc-L-methionine-methyl ester + H2O2
Boc-L-methionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
show the reaction diagram
-
i.e. monochlorodimedone
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-
?
cis-2-hexen-1-ol + tert-butyl hydroperoxide
cis-2-hexenal + ?
show the reaction diagram
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further production of small amounts of trans-2-hexenal, cis-3-hexenal and trans-3-hexenal
-
?
cis-2-phenylcyclopropylmethanol + tert-butyl hydroperoxide
?
show the reaction diagram
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-
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-
?
cis-3-hexen-1-ol + tert-butyl hydroperoxide
cis-3-hexenal + ?
show the reaction diagram
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-
further production of small amounts of cis-2-hexenal, trans-2-hexenal and trans-3-hexenal
-
?
cis-4-hexen-1-ol + tert-butyl hydroperoxide
cis-4-hexenal + cis-4,5-epoxyhexan-1-ol + ?
show the reaction diagram
-
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further production of small amounts of trans-4,5-epoxyhexan-1-ol and trans-4-hexenal
-
?
cis-beta-methylstyrene + chloride + H2O2
?
show the reaction diagram
-
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the enzyme produced (1S2R)- and (1R2S)-epoxides at a 96:4 product ratio
-
?
cis-cyclohexa-3,5-diene-1,2-diol + tert-butyl hydroperoxide
(1R,2S,3S,4S)-cyclohex-5-ene-1,2,3,4-tetrol + ?
show the reaction diagram
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+ traces of (1R,2S,3S,6S)-7-oxabicyclo[4.1.0]hept-4-ene-2,3-diol
-
?
Cl2O2 + H+
Cl- + ClO2 + H2O
show the reaction diagram
-
dismutation
-
?
ClO2 + H2O
Cl- + ClO3- + O2 + H+
show the reaction diagram
-
dismutation
-
?
cytidine + Br- + H2O2
5-bromocytidine + H2O
show the reaction diagram
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-
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?
cytosine + Br- + H2O2
?
show the reaction diagram
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-
-
-
?
fluoranthene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
fluorene + Cl- + H2O2
dichlorofluorene + H2O
show the reaction diagram
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-
-
?
geraniol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
guanosine + Br- + H2O2
8-bromoguanosine + H2O
show the reaction diagram
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-
-
?
H2O2
H2O + O2
show the reaction diagram
-
-
-
?
H2O2 + methylene blue
oxidized methylene blue + H2O
show the reaction diagram
-
-
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?
indole + chloride + H2O2
?
show the reaction diagram
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-
-
-
?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
show the reaction diagram
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-
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-
?
indole + H2O2
2-oxindole + H2O
show the reaction diagram
indole + H2O2
2-oxoindole + H2O
show the reaction diagram
indole + tert-butyl hydroperoxide
2-oxoindole + ?
show the reaction diagram
-
-
-
-
?
isoplagiochin C + Cl- + H2O2
?
show the reaction diagram
Met + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
monochlordimedone + KCl + H2O2 + tert-butyl hydroperoxide
?
show the reaction diagram
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-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
show the reaction diagram
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
show the reaction diagram
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
show the reaction diagram
monochlorodimedone + Cl- + H2O2
dichlorodimedone + H2O
show the reaction diagram
monochlorodimedone + H2O2 + HCl
dichloromedone + H2O
show the reaction diagram
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-
-
-
?
monochlorodimedone + HCl + H2O2
?
show the reaction diagram
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-
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?
monochlorodimedone + KCl + H2O2
?
show the reaction diagram
-
cross-linked enzyme aggregates
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-
?
monochlorodimedone + KCl + H2O2
dichlorodimedone + KOH + H2O
show the reaction diagram
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-
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?
N,N,N',N'-tetramethylphenylene diamine + H2O2 + HCl
?
show the reaction diagram
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-
-
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?
N-acetyl-L-methionine-methyl ester + H2O2
N-acetyl-L-methionine-methyl ester (RS)-sulfoxide
show the reaction diagram
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-
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?
N-chloroacetyl-L-methionine-methyl ester + H2O2
N-chloroacetyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-formyl-L-methionine-methyl ester + H2O2
N-formyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
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?
N-methoxycarbonyl-D-ethionine-methyl ester + H2O2
N-methoxycarbonyl-D-ethionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
N-methoxycarbonyl-D-methionine-ethyl ester + H2O2
N-methoxycarbonyl-D-methionine-ethyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-D-methionine-methyl ester + H2O2
N-methoxycarbonyl-D-methionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
N-methoxycarbonyl-D-methionine-n-butyl ester + H2O2
N-methoxycarbonyl-D-methionine-n-butyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-D-methionine-n-propyl ester + H2O2
N-methoxycarbonyl-D-methionine-n-propyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-L-ethionine-ethyl ester + H2O2
N-methoxycarbonyl-L-ethionine-ethyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-L-ethionine-methyl ester + H2O2
N-methoxycarbonyl-L-ethionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-L-methionine-ethyl ester + H2O2
N-methoxycarbonyl-L-methionine-ethyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-L-methionine-methyl ester + H2O2
N-methoxycarbonyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-butyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-butyl ester (RS)-sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-pentyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-pentyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
N-methoxycarbonyl-L-methionine-n-propyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-propyl ester (RS)-sulfoxide + H2O
show the reaction diagram
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-
-
-
?
naphthalene + Cl- + H2O2
?
show the reaction diagram
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-
-
-
?
naphthalene + KCl + H2O2
chloronaphthalene + KOH + H2O
show the reaction diagram
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-
-
-
?
nerol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
p-nitrostyrene + H2O2
p-nitrostyrene oxide + H2O
show the reaction diagram
-
-
-
-
?
pentachlorophenol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
pentachlorophenol + HCl + H2O
?
show the reaction diagram
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
perylene + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
phenanthrene + Cl- + H2O2
chlorophenanthrene + H2O
show the reaction diagram
-
-
-
?
pyrazole + Br- + H2O2
4-bromopyrazole + H2O
show the reaction diagram
-
-
-
?
pyrazole + Cl- + H2O2
4-chloropyrazole + H2O
show the reaction diagram
-
-
-
?
pyrazole + I- + H2O2
4-iodopyrazole + H2O
show the reaction diagram
-
-
-
?
pyrene + Cl- + H2O2
chloropyrene + dichloropyrene + H2O
show the reaction diagram
-
-
-
?
pyrogallol + chloride + H2O2
?
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
-
-
-
-
?
RH + chloride + H2O2
RCl + H2O
show the reaction diagram
-
-
-
-
?
styrene + H2O2
?
show the reaction diagram
-
native enzyme is conjugated with polystyrene to form a surfactant-like structure that self assembled at oil-water interfaces. The interface-assembly of the enzyme improves the overall catalytic efficiency as compared to traditional biphasic reactions with enzymes contained in bulk aqueous phase. The interfacial placement of the enzyme can suppress unwanted side reactions including the hydrolysis of the styrene epoxide product
-
-
?
styrene + tert-butyl hydroperoxide
styrene oxide + ?
show the reaction diagram
-
-
-
-
?
sulfur mustard + chloride + H2O2
sulfur mustard sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
thianthrene + H2O2 + Cl-
?
show the reaction diagram
-
-
-
-
?
thioanisole + H2O2
(R)-methyl phenyl sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
thioanisole + H2O2
?
show the reaction diagram
-
-
-
-
?
thioanisole + H2O2
methyl phenyl sulfoxide + H2O
show the reaction diagram
-
-
-
-
?
thioanisole + H2O2
methyl-phenyl sulfoxide + ?
show the reaction diagram
-
-
-
?
thioanisole + H2O2 + Cl-
?
show the reaction diagram
-
-
-
-
?
thioanisole + HCl + H2O2
?
show the reaction diagram
-
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
-
-
?
thiourea + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
thymine + Br- + H2O2
5-bromo-6-hydroxy-5,6-dihydrothymine + H2O
show the reaction diagram
-
-
-
?
trans-2-hexen-1-ol + tert-butyl hydroperoxide
trans-2-hexenal + ?
show the reaction diagram
-
-
further production of small amounts of cis-2-hexenal,cis-3-hexenal and trans-3-hexenal
-
?
trans-2-phenylcyclopropylmethanol + tert-butyl hydroperoxide
?
show the reaction diagram
-
formation of the aldehyde with poor enantioselectivity
-
-
?
trans-3,4-dimethoxycinnamic acid + Br- + H2O2 + H+
DL-1,1-dibromo-2-hydroxy-2-(3,4-dimethoxy-5-bromophenyl)ethane + DL-1,1-dibromo-2-hydroxy-2-(3,4-dimethoxyphenyl)ethane + 2-bromo-3-hydroxy-3-(3,4-dimethoxyphenyl)propionic acid + H2O
show the reaction diagram
-
-
-
?
trans-3,4-dimethoxycinnamic acid + Cl- + H2O2 + H+
trans-1-chloro-2-(3,4-dimethoxy-5-chlorophenyl)ethylene + trans-1-chloro-2-(3,4-dimethoxyphenyl)ethylene + DL-1,1-dichloro-2-hydroxy-2-(3,4-dimethoxyphenyl)ethane
show the reaction diagram
-
-
-
?
trans-3-hexen-1-ol + tert-butyl hydroperoxide
trans-3-hexenal + ?
show the reaction diagram
-
-
further production of small amounts of cis-3-hexenal, trans-2-hexenal and cis-3-hexenal
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-2-(3-ethyloxiran-2-yl)ethanol + (3E)-hex-3-enal + H2O
show the reaction diagram
-
-
-
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-4,5-epoxyhexan-1-ol + trans-4-hexenal + H2O + ?
show the reaction diagram
-
-
-
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-4-hexenal + trans-4,5-epoxyhexan-1-ol + ?
show the reaction diagram
-
-
further production of small amounts of cis-4,5-epoxyhexan-1-ol and cis-4-hexenal
-
?
trans-4-hydroxycinnamic acid + Br- + H+ + H2O2
trans-1-bromo-2-(4-hydroxyphenyl)ethylene + H2O
show the reaction diagram
-
-
-
?
trans-4-hydroxycinnamic acid + Cl- + H+ + H2O2
trans-1-chloro-2-(4-hydroxyphenyl)ethylene + H2O
show the reaction diagram
-
-
-
?
trans-4-methoxy-cinnamic acid + Br- + H+ + H2O2
2,3-dihydroxy-3-(4-methoxyphenyl)propionic acid + DL-1,1-dibromo-2-hydroxy-2-(4-methoxyphenyl)ethane + H2O
show the reaction diagram
-
-
-
?
trans-cinnamic acid + H2O2 + Br- + H+
trans-1-bromo-2-phenylethylene + erythro-2-bromo-3-hydroxy-3-phenylpropionic acid + H2O
show the reaction diagram
-
-
-
?
triphenylene + Cl- + H2O2
chlorotriphenylene + H2O
show the reaction diagram
-
-
-
?
tyrosine + Br- + H2O2
?
show the reaction diagram
-
-
-
-
?
tyrosine + Br- + H2O2
monobromotyrosine + dibromotyrosine
show the reaction diagram
-
-
-
?
tyrosine + Cl- + H2O2
monochlorotyrosine + dichlorotyrosine
show the reaction diagram
-
-
-
?
tyrosine + I- + H2O2
?
show the reaction diagram
-
-
-
-
?
uracil + Br- + H2O2
5-bromouracil + H2O
show the reaction diagram
-
-
-
?
uracil + Cl- + H2O2
5-chlorouracil + H2O
show the reaction diagram
-
-
-
?
uracil + I- + H2O2
5-iodouracil + H2O
show the reaction diagram
-
-
-
?
[2-(2-bromoethyl)cyclopropyl]methanol + tert-butyl hydroperoxide
2-(2-bromoethyl)cyclopropanecarbaldehyde + ?
show the reaction diagram
-
-
-
-
?
[2-(3-bromopropyl)cyclopropyl]methanol + tert-butyl hydroperoxide
2-(3-bromopropyl)cyclopropanecarbaldehyde + ?
show the reaction diagram
-
-
-
-
?
[2-(hydroxymethyl)cyclopropyl]methyl acetate + tert-butyl hydroperoxide
(2-formylcyclopropyl)methyl acetate + ?
show the reaction diagram
-
-
-
-
?
[3.2.0]hept-2-en-6-one + Br- + H2O2
2-exo-bromo-3-endo-hydroxybromohydrin + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
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
2,3,5,6-tetrachlorophenol + Cl- + H2O2
pentachlorophenol + H2O
show the reaction diagram
-
-
-
-
?
2,4-dichlorophenol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
4-chlorophenol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
4-fluorophenol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
pentachlorophenol + Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
RH + chloride + H2O2
RCl + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
transformation of aromatic pollutants into chlorinated derivatives by microbial enzymes may occur in polluted sites. This biocatalytic process should be considered because the toxicity and environmental impact of aromatic compounds may be increased
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme does not require any cofactor for its activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-vinyl-2-oxazolidinethione
-
-
azide
diethyl dicarbonate
-
the covalent modification of His105 inhibits the epoxidation and peroxide dismutations catalyzed by CPO
dimethyl dicarbonate
-
the covalent modification of His105 inhibits the epoxidation and peroxide dismutations catalyzed by CPO
hydrogen peroxide
-
the main process leading to peroxide-mediated enzyme inactivation is heme destruction (all tryptophan residues are partially oxidized in the inactive protein). 80000 molar equivalents of hydrogen peroxide are sufficient to reduce the activity of CPO to less than 5%
Sodium cyanoborohydride
-
activity decreases in 38.2 and 92.6% for sodium cyanoborohydride molar excess of 1:1000 and 1:10000
tert-butyl hydroperoxide
-
kinetic studies
thiouracil
-
-
Thiourea
-
competitive with halogen acceptor
additional information
-
not inhibited by sodium cyanoborohydride in molar excess of 1:10 and 1:100
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
enhances total turnover number compared to reaction without antioxidant
azide
-
at pH 4.0, infra-micromolar concentrations of azide enhance enzyme activity
caffeic acid
-
the total turnover number is almost 5fold higher than that obtained for the reference reaction
Cetyltrimethylammonium bromide
-
the peroxidation activity of CPO is enhanced by 248% while oxidation activity is enhanced by 215% in cetyltrimethylammonium bromide reverse micelle medium
citraconic anhydride
-
the catalytic efficiency of the modified enzyme for sulfoxidation in aqueous buffer is increased by 26.2%
dodecyltrimethylammonium bromide
-
the peroxidation activity of CPO is enhanced by 263%, while oxidation activity is enhanced by 222% in dodecyltrimethylammonium bromide medium
ferulic acid
-
enhances total turnover number compared to reaction without antioxidant
ionic liquids
-
enhanced activity in ionic liquids
-
Maleic anhydride
-
the catalytic efficiency of the modified enzyme for sulfoxidation in aqueous buffer is increased by 22.6%
phthalic anhydride
-
the catalytic efficiency of the modified enzyme for sulfoxidation in aqueous buffer is increased by 12.9%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038
2,3,5,6-tetrachloroaniline
-
-
0.006
2,3,5,6-Tetrachlorophenol
-
-
770
4-chloroaniline
-
pH 4.4, 30C
10
Chlorite
-
-
0.03 - 154
H2O2
0.0261 - 0.0277
Monochlorodimedon
0.02
monochlorodimedone
-
in 50 mM phosphate buffer pH 2.75 at 30C, with 20 mM KCl
0.12
Pentachlorophenol
-
-
0.089
pyrogallol
-
in 50 mM phosphate buffer pH 2.75 at 30C, with 20 mM KCl
0.0001 - 0.00036
R-(+)-limonene
195 - 1668
Styrene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 18.7
(R)-limonene
35.95
2,3,5,6-tetrachloroaniline
Leptoxyphium fumago
-
-
60.8
2,3,5,6-Tetrachlorophenol
Leptoxyphium fumago
-
-
11.28
2,4,6-Trichlorophenol
Leptoxyphium fumago
-
in 0.1 M acetate buffer pH 5.0, at 25C
123 - 661.1
4,6-dimethyldibenzothiophene
7.2 - 8
anthracene
70000
Chlorite
Leptoxyphium fumago
-
-
1.64
monochlorodimedone
Musa x paradisiaca
-
in 50 mM phosphate buffer pH 2.75 at 30C, with 20 mM KCl
3.6 - 4.5
Naphthalene
46.97
Pentachlorophenol
Leptoxyphium fumago
-
-
46 - 56.6
pyrene
26.56
pyrogallol
Musa x paradisiaca
-
in 50 mM phosphate buffer pH 2.75 at 30C, with 20 mM KCl
4.9 - 30.9
Styrene
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
82
monochlorodimedone
Musa x paradisiaca
-
in 50 mM phosphate buffer pH 2.75 at 30C, with 20 mM KCl
3888
298.4
pyrogallol
Musa x paradisiaca
-
in 50 mM phosphate buffer pH 2.75 at 30C, with 20 mM KCl
658
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.27
-
crude enzyme, at pH 2.75 and 30C
2.25
-
after 8.33fold purification, at pH 2.75 and 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4 - 3
-
soluble enzyme and immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
2.5
-
with monochlorodimedone as substrate
2.7 - 5
-
wild-type enzyme, chlorination activity
3.8
-
pH optimum for CPO adsorbed on SBA-15
4 - 6
-
soluble and immobilized enzyme
4.5 - 5.5
-
-
4.8
-
halide ion independent evolution of oxygen from hydrogen peroxide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 4
-
pH 2.0: about 60% of maximal acticity of soluble enzyme, about 65% of maximal activity of immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads). pH 4.0: about 55% of maximal activity of soluble enzyme, about 75% of maximal activity of immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
2 - 5
-
free and bio-conjugated-CPO poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane
2.5 - 5
-
mainly
3 - 4
-
at pH values lower than 3.0 or higher than 4.0, the enzyme is completely inhibited
3.7 - 7
-
pH 3.7: about 90% of maximal activity, soluble and immobilized enzyme. pH 7.0: about 55% of maximal activity of immobilized enzyme, about 50% of maximal activity of soluble enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2 - 4
-
values of the isoenzymes
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32974
-
x * 32974, calculation from nucleotide sequence
40000
-
chloroperoxidase B, gel filtration
42882
-
2 * 42882, ESI-MS after SDS-PAGE
43000
-
x * 43000, SDS-PAGE
46000
-
chloroperoxidase A, gel filtration
109000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 42882, ESI-MS after SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chloroperoxidase A and B
-
hanging drop method, crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate
-
sitting drop vapor diffusion method, crystals are modified by several cross-linkers, but only glutaraldehyde is able to produce catalytically active and insoluble crystals. Although the cross-linked crystals are catalytically active, they show lower specific activity than the soluble enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5
-
4C, stable for several h
348317
2.5 - 6
-
at pH 2.75 it loses 85% activity in 1 h, and it is completely inactivated in 24 h. At pH 4.4, the enzyme also loses activity with time and is completely inactivated after 2.5 h. However, the enzyme exposed to pH 6.0 has low activity but it remains constant for 24 h
725151
2.8 - 6
-
25C, 24 h, immobilized and soluble enzyme are stable
659741
3 - 6.5
-
4C, in presence of 0.1 M fluoride, stable for several days
348317
5 - 5.8
-
-
696905
5 - 6.5
-
at pH 6.5 the soluble enzyme retains about 70% of initial activity after 3 days of incubation, while at both pH 6.0 and 5.0 the enzyme retains more than 95%
725740
7
-
25C, 24 h, about 50% loss of activity of soluble enzyme, about 40% loss of activity of immobilized enzyme
659741
7.6
-
after 1 h: 50% residual ativity for cross-linked enzyme aggregates, complete inactivation of free enzyme
695425
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
enzyme in ternary system P1a: 65% residual activity after 24h
35
-
at 35C, the reaction rate initially increases, but the enzyme rapidly becomes inactivated and the reaction rate decreases
40 - 50
-
thermostability is greatly improved in a reverse micelle composed of surfactant-water-isooctane-pentanol: at 40C, CPO essentially loses all its activity after 5h incubation, while 58-76% catalytic activity is retained for both reactions in the two reverse micelle media. At 50C, about 44-75% catalytic activity remains for both reactions in reverse micelle after 2h compared with no observed activity in pure buffer under the same conditions
45 - 55
-
at 45C, the conjugated-CPO preserved loses about 7% of its initial activity whereas the free enzyme loses about 34% of its initial activity during a 120 min incubation period. At 55C, the conjugated-CPO and free CPO retain their activity about to a level of 53% and 11%, respectively
70
-
1 h, about 10% loss of activity of crystals cross-linked with glutaraldehyde and more than 95% loss of activity of soluble enzyme
80
-
1 h, about 95% loss of activity of crystals cross-linked with glutaraldehyde and complete than 90% loss of activity of soluble enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.3 mM H2O2, 20 h: 58% activity for immobilized enzyme, 43% activity for free enzyme
-
1.5 M urea, 20 h: 99% activity for immobilized enzyme, 68% activity for free enzyme
-
15 mM H2O2, 5 min: complete inactivation of free enzyme
-
30 mM H2O2, 5 min: 80% residual activity for the cross-linked enzyme aggregates
-
addition of poly(ethylene glycol) results in an increase of 57% for interface-bound CPO and 33% for native enzyme
-
addition of polyethyleneimine results in enhancement of storage stability against H2O2 deactivation, but does not affect the operational stability of the enzyme
-
covalently bonded CPO on the mesoporous material SBA-15 exhibits a higher operational stability in a continuously operated fixed-bed reactor compared to a catalyst prepared by physisorption of the enzyme. Chloroperoxidase immobilization into SBA-15 shows a remaining activity of about 9%
-
cross-linked enzyme aggregates exhibit greatly improved stability in the presence of H2O2
-
crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme
-
di(ethylene glycol) and di(propylene glycol) stabilize the enzyme towards denaturation by H2O2
-
enhanced stability in ionic liquids
-
enzyme immobilized on monoaminoethyl-N-aminoethyl through carbodiimide-coupled method shows an increase in apparent half-life time of more than 500fold that of the soluble enzyme
-
glucose enhances the operational stability by two folds, but exhibits no significant effect on storage stability
-
immobilization of chloroperoxidase to silica gel in order to increase its stability either in buffer solution or in the presence of the oxidant tert-butyl hydroperoxide. The binding between enzyme and silica gel results in a non-homogeneous enzyme population. Existence of three different enzyme populations. Two populations of the immobilized enzyme show an apparent increase in the stability both to the pH or to the presence of the oxidant
-
immobilization of the enzyme on silica gel enhances the stability with respect to the effect of pH and oxidizing agent concentrations
-
immobilized CPO (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) retains 83% of its initial activity after 12 cycles of usage
-
interface-assembled enzyme shows improved stability as compared to native enzyme, enzyme deactivation as a result of the side effect of H2O2, still limits the overall productivity of the enzyme
-
PEG200 and glycerol are the most efficient stabilizer for CPO in temperatures ranging from 25C to 60C. Trehalose is more helpful than other sugars for extended storage of CPO
-
stability of the immobilized CPO (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) is improved compared to free form
-
stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide
-
the catalytic efficiency of free CPO is decreased about 1.6fold upon immobilization. The conjugated-CPO activity on the poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane remains almost the same as the original activity after 9 cycles. After that, a steady decrease in chlorination capability of the conjugated-CPO is observed, and this loss reaches about 27% after 25 cycles of batch operation
-
the enzyme tolerates up to 30% v/v 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate
-
the thermostability of peroxidase of CPO is increased about 2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride. The thermostability of sulfoxidation activity of CPO is increased about 1.2fold upon the chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,3-dimethylimidazolium methylsulfate
-
the enzyme tolerates up to 30% v/v in citrate buffer system, activity is retained for 24 h
1-butyl-3-methylimidazolium methylsulfate
-
the enzyme tolerates up to 30% v/v in cytitrate buffer system, activity is retained for 24 h
Acetone
-
loss of activity after 3 h
tert-Butanol
-
loss of activity after 3 h
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
tert-butyl hydroperoxide, 10 mM, soluble enzyme is almost completely inactive after 2 h, immobilized enzyme still retains 20% of its activity after 4 h. After 24 h in 0.1 mM tert-butyl hydroperoxide the activity of immobilized enzyme is unaffected, while soluble enzyme loses more than 50% of its original activity
-
659741
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, pH 6.0, half-life of autoxidation of the oxygenated heme protein is 20 min
-
-20C, pH 6, less than 20% loss of activity after 6 months
-
-20C, pH 6.0, half-life of autoxidation of the oxygenated heme protein is 85 min
-
4C, citrate buffer (50 mM, pH 3.0), 4 weeks, 91% loss of activity of the soluble enzyme, immobilized (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) enzyme loses 15% of its initial activity
-
4C, conjugated-CPO in citrate buffer (50 mM, pH 3.0), 8 weeks, the conjugated-CPO preserves its initial activity more than 60%
-
4C, CPO immobilized into glutaraldehyde-3-aminopropyltrimethoxysilane-SBA-15 in a buffer at pH 3.4, storage results in leaching of the enzyme from the support due to hydrolytic cleavage of the imino bond
-
4C, CPO immobilized into glutaraldehyde-3-aminopropyltrimethoxysilane-SBA-15 in a buffer at pH 7.0, a few days, complete loss of enzyme activity
-
4C, free and conjugated-CPO in citrate buffer (50 mM, pH 3.0), 4 weeks, the activity loss of the conjugated-CPO is 7% while the free enzyme loses its initial activity about 83%
-
4C, free enzyme in citrate buffer (50 mM, pH 3.0), 6 weeks, the free enzyme loses all its activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a simple four-step procedure; chloroperoxidase A and B
-
chloroperoxidase A and B
-
recombinant enzyme
-
ultrafiltration and DEAE cellulose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus niger
-
expression of E183H in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E183H
-
the mutation is detrimental to the chlorination and dismutation activity of chloroperoxidase, activities are reduced by 85% and 50% of the wild-type activity. Epoxidation activity of the mutant enzyme is significantly enhanced, about 2.5fold
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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CPO is used as a versatile biological catalyst
environmental protection
synthesis
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