1.11.1.10: chloride peroxidase
This is an abbreviated version!
For detailed information about chloride peroxidase, go to the full flat file.
Word Map on EC 1.11.1.10
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1.11.1.10
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fumago
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caldariomyces
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horseradish
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chlorination
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peroxidases
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halogen
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halide
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haloperoxidase
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bromination
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lactoperoxidase
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inaequalis
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ferryl
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curvularia
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soret
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bromoperoxidase
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monochlorodimedone
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low-spin
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p450cam
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vanadium-dependent
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thioanisole
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peroxidase-catalyzed
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thiolate-ligated
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pyrrocinia
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oxoferryl
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n,n-dimethylaniline
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peroxygenases
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agrocybe
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vanadium-containing
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hypohalous
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aegerita
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degradation
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synthesis
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environmental protection
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biotechnology
- 1.11.1.10
- fumago
-
caldariomyces
- horseradish
-
chlorination
- peroxidases
-
halogen
- halide
- haloperoxidase
-
bromination
- lactoperoxidase
- inaequalis
-
ferryl
-
curvularia
-
soret
-
bromoperoxidase
- monochlorodimedone
-
low-spin
-
p450cam
-
vanadium-dependent
- thioanisole
-
peroxidase-catalyzed
-
thiolate-ligated
- pyrrocinia
-
oxoferryl
- n,n-dimethylaniline
-
peroxygenases
-
agrocybe
-
vanadium-containing
-
hypohalous
- aegerita
- degradation
- synthesis
- environmental protection
- biotechnology
Reaction
Synonyms
CCPO, Chloride peroxidase, chloroperoxidase, chloroproxidase, CPO, CPO-I, CPO2, haeme-thiolate peroxidase, heme-containing CPO, heme-thiolate chloroperoxidase, More, peroxidase, chloride, Vanadium chloride peroxidase, vCPO
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General Information on EC 1.11.1.10 - chloride peroxidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Removal of the sugars from CPO leads to increase the hydrophobicity of the enzyme, as well as the reduction of the alkylation reactions
physiological function
additional information
evolution
Caldariomyces fumago chloroperoxidase (CPO) is a glycosylated hemoprotein enzyme from the peroxidase family
evolution
chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme of the peroxidase family
evolution
chloroperoxidase (CPO) is a hybrid of two different families of enzymes, peroxidases and P450s
physiological function
chloroperoxidase (CPO) is a heme-thiolate enzyme able to catalyse the halogenation and oxidation of a wide range of organic substrates. CPO-catalysed chlorination and bromination reaction of natural estrogens, beta-estradiol, estrone and equiline are efficiently converted to halogenated compounds in the presence of chloride or bromide and hydrogen peroxide. The bromination reaction proceeds more efficiently than the chlorination reaction. Three major products are detected for chlorination of beta-estradiol, two of them are monohalogenated compounds while a third product is a dihalogenated compound at positions 2 and 4 of the aromatic ring A. Chlorinated compounds are not substrates for tyrosinase, suggesting that the halogenated form of estrogens is less susceptible to form o-quinones. Chlorinated estradiol is not a substrate of tyrosinase. Whereas E2 is completely consumed in the presence of tyrosinase, E2-derived chlorinated compounds are not transformed. 2,4-Dichloroestradiol is 90fold less estrogenic compared to beta-estradiol
physiological function
chloroperoxidase (CPO), secreted by the marine fungus Caldariomyces fumago, is a versatile enzyme with the capacity to catalyze the incorporation of halogen atoms into organic molecules in the presence of peroxides such as H2O2. Production of polyhalogenated carbazoles (PHCs) from halogenation of carbazole in the presence of bromide and/or chloride under the catalysis of chloroperoxidase (CPO) isolated from the marine fungus Caldariomyces fumago. CPO-catalyzed halogenation of carbazole may play an important role in the natural formation of PHCs. PHCs exhibit dioxin-like toxicity and are persistent and bioaccumulative. PHCs induce cytochrome P450 enzymes and certain other enzyme activities. The chlorinated and brominated carbazoles produced in the reactions with Cl- and Br- in vitro are also found in aquatic environments, overview
physiological function
chloroperoxidase (CPO), which is a versatile heme-containing enzyme, can catalyze sulfoxidation, epoxidation, dismutation, halogenation, and oxidation of numerous compounds with extensive high regioselectivity and enantioselectivity
physiological function
containing both a P450-like proximal pocket and a peroxidase-like distal pocket, enzyme chloroperoxidase (CPO) is a versatile heme-containing enzyme that possesses the catalytic capacities of both peroxidase and P450 enzyme families. CPO has multiple catalytic functions, attributable to four CPO-mediated processes, including bromination, radical coupling, intramolecular cyclization and debromination. Phenol is readily transformed into a variety of brominated organic compounds (BOCs) via the CPO-mediated oxidative process. Higher bromide concentrations and lower pH conditions both facilitate the formation of brominated products. While a higher bromination capacity is observed in pH 3.0 solutions, CPO-mediated radical couplings are more favorable at pH 5.0 and pH 6.0. Although CPO might catalyze chlorination when chloride and bromide coexisted in the solution, BOCs are the dominant products of CPO-mediated phenol oxidation. Bromination (EC 1.11.1.18) is preferable to chlorination (EC 1.11.1.10) in the CPO-mediated reaction in the presence of both bromide and chloride
physiological function
the heme-containing CPO exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing the halogenation reactions. CPO selectively causes the oxidation and epoxidation of the diverse chemical compounds through the specific stereochemistry mechanism
physiological function
the immobilized enzyme CPO catalyzes degradation of mesotrione (2-[(4-methylsulfonyl)-2-nitrobenzoyl]cyclohexan-1,3-dione) in wastewater
additional information
analysis of the effect of 1-butyl-3-methylimidazolium bromide ([BMIM][Br]) and 1-butyl-3-methylimidazolium methyl sulfate ([BMIM] [MeSO4]) ionic liquids on the structure and function of chloroperoxidase (CPO) by molecular dynamics (MD) simulation using the enzyme structure (PDB ID 2CPO) as template, detailed overview. [BMIM][MeSO4] possesses greater influence on the enzyme structure, because of the special structure of the corresponding anion group. Besides, the number of cavities interprets the activation of the enzyme at the low concentrations and its inactivation at the high concentrations. The penetration of the anions into the enzyme structure is confirmed at the high concentrations of the ionic liquids. The role of ionic liquids at low concentrations is related to their binding to the enzyme structure. Their role at the high concentrations depends on the changes in the solvent arrangement as well as the attachment to the enzyme. Low concentration of ionic liquid play an important role and cause higher chloroproxidase activity.Whereas in high concentration due to surface coating of chloroproxidase by ionic liquid, despite the access of the substrate to the active site, CPO activity decreases. In chloroperoxidase, the substrate accesses the active site and heme group through a small channel above heme
additional information
computational molecular dynamics calculation, simulation, and modeling, using the glycosylated enzyme structure PDB ID 2CPO, overview
additional information
substrate specificity via hybrid quantum mechanics/molecular mechanics (QM/MM) calculation and simulation, modeling and structure-function analysis, overview. The influence of the NH-S hydrogen bonds on the full reaction profiles for hydroxylation and epoxidation has been studied by density functional theory (DFT) calculations on small heme-thiolate models that incorporate ammonia molecules hydrogen bonded to a proximal SH- group. The proximal pocket is the key determinant of alkene oxidation selectivity. The selectivity for epoxidation can be rationalized in terms of the proximal pocket's modulation of the thiolate's electron push and consequent influence on the heme redox potential and the basicity of the trans ligand. Creation of two active-site models for each substrate/enzyme combination, one with a bare heme-thiolate and one that also includes the proximal pocket, so that comparison of the PES's reveals the influence of the proximal pocket on the intrinsic reactivity
