ID   1.11.1.10
DE   chloride peroxidase.
AN   chloroperoxidase.
AN   CPO.
AN   vanadium haloperoxidase.
CA   RH + Cl(-) + H2O2 = RCl + 2 H2O.
CC   -!- Brings about the chlorination of a range of organic molecules,
CC       forming stable C-Cl bonds.
CC   -!- Also oxidizes bromide and iodide.
CC   -!- Enzymes of this type are either heme-thiolate proteins, or contain
CC       vanadate.
CC   -!- A secreted enzyme produced by the ascomycetous fungus Caldariomyces
CC       fumago (Leptoxyphium fumago) is an example of the heme-thiolate type.
CC   -!- It catalyzes the production of hypochlorous acid by transferring one
CC       oxygen atom from H2O2 to chloride.
CC   -!- At a separate site it catalyzes the chlorination of activated
CC       aliphatic and aromatic substrates, via HClO and derived chlorine
CC       species.
CC   -!- In the absence of halides, it shows peroxidase (e.g. phenol
CC       oxidation) and peroxygenase activities.
CC   -!- The latter inserts oxygen from H2O2 into, for example, styrene (side
CC       chain epoxidation) and toluene (benzylic hydroxylation), however,
CC       these activities are less pronounced than its activity with halides.
CC   -!- Has little activity with non-activated substrates such as aromatic
CC       rings, ethers or saturated alkanes.
CC   -!- The chlorinating peroxidase produced by ascomycetous fungi (e.g.
CC       Curvularia inaequalis) is an example of a vanadium chloroperoxidase,
CC       and is related to bromide peroxidase (EC 1.11.1.18).
CC   -!- It contains vanadate and oxidizes chloride, bromide and iodide into
CC       hypohalous acids.
CC   -!- In the absence of halides, it peroxygenates organic sulfides and
CC       oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)]
CC       but no phenols.
DR   P49053, PRXC_CURIN ;  P04963, PRXC_LEPFU ;
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