CATH Classification

Domain Context

CATH Clusters

Superfamily Chloroperoxidase-like
Functional Family Chloroperoxidase

Enzyme Information
Chloride peroxidase.
based on mapping to UniProt P04963
RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
-!- 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 catalyzes the production of hypochlorous acid by transferring one oxygen atom from H(2)O(2) to chloride. -!- At a separate site it catalyzes 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 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. -!- 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 -!- 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.

UniProtKB Entries (1)

Leptoxyphium fumago

PDB Structure

External Links
Primary Citation
The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
Sundaramoorthy, M., Terner, J., Poulos, T.L.