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Literature summary for 1.11.1.18 extracted from

  • Wang, K.; Huang, X.; Lin, K.
    Multiple catalytic roles of chloroperoxidase in the transformation of phenol products and pathways (2019), Ecotoxicol. Environ. Saf., 179, 96-103 .
    View publication on PubMed

Application

Application Comment Organism
environmental protection CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters Leptoxyphium fumago

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,4-dibromophenol + bromide + H2O2 Leptoxyphium fumago
-
2,4,6-tribromophenol + 2 H2O
-
?
4-bromophenol + bromide + H2O2 Leptoxyphium fumago
-
2,4-dibromophenol + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago P04963 Caldariomyces fumago
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,4-dibromophenol + bromide + H2O2
-
Leptoxyphium fumago 2,4,6-tribromophenol + 2 H2O
-
?
4-bromophenol + bromide + H2O2
-
Leptoxyphium fumago 2,4-dibromophenol + 2 H2O
-
?
additional information H2O2 activation of the heme group. LC-MS/MS and gas chromatography-mass spectrometry (GC-MS) are used for product identification, overview. 2,2'-Dihyroxy-3,3',5,5'-tetrabromobiphenyl is also formed in the reactions, but is no substrate itself, no activity with 2,4,6-tribromophenol as a substrate. Evolution of BOC formation from phenol during CPO-mediated oxidation in the presence of bromide overview. Hydroxylated polybrominated diphenyl ethers (diOH-PBDEs) and hydroxylated polybrominated biphenyls (diOH-PBBs) formed by dihydroxyl group substitutions in the ortho-positions relative to the diphenyl ether bond or the single bond in biphenyl, may undergo intramolecular cyclization Leptoxyphium fumago ?
-
-
phenol + bromide + H2O2
-
Leptoxyphium fumago 4-bromophenol + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
More see also EC 1.11.1.10 Leptoxyphium fumago

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Leptoxyphium fumago

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
-
Leptoxyphium fumago

pH Range

pH Minimum pH Maximum Comment Organism
3 7 CPO has preferential enzymatic activities under different pH conditions Leptoxyphium fumago

Cofactor

Cofactor Comment Organism Structure
heme H2O2 activation of the heme group Leptoxyphium fumago

General Information

General Information Comment Organism
evolution chloroperoxidase (CPO) is a hybrid of two different families of enzymes, peroxidases and P450s Leptoxyphium fumago
metabolism proposed pathways for the chloroperoxidase-catalyzed oxidation of phenol in the presence of bromide, overview Leptoxyphium fumago
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. Proposed pathways for the chloroperoxidase-catalyzed oxidation of phenol in the presence of bromide, overview Leptoxyphium fumago