×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Chloroperoxidase-like
Functional Family

Enzyme Information

1.11.1.10
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 1.11.1.18). -!- 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)

P04963
PRXC_LEPFU
Leptoxyphium fumago
Chloroperoxidase

PDB Structure

PDB 2J5M
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure and Quantum Chemical Characterization of Chloroperoxidase Compound 0, a Common Reaction Intermediate of Diverse Heme Enzymes.
Kuhnel, K., Derat, E., Terner, J., Shaik, S., Schlichting, I.
Proc.Natl.Acad.Sci.USA
CATH-Gene3D is a Global Biodata Core Resource Learn more...