CPO

Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds.

Source:http://purl.uniprot.org/enzyme/1.11.1.10

Statements in which the resource exists as a subject.
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A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type., Also oxidizes bromide and iodide., At a separate site it catalyzes the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species., Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds., Enzymes of this type are either heme-thiolate proteins, or contain vanadate., Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes., In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS (2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)) but no phenols., In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities., It catalyzes the production of hypochlorous acid by transferring one oxygen atom from H(2)O(2) to chloride., It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids., 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)., The latter inserts oxygen from H(2)O(2) into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides.
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uniprot:name
CPO, Chloride peroxidase, Chloroperoxidase, Vanadium haloperoxidase
uniprot:activity
RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
uniprot:cofactor
Heme