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CATH Superfamily 1.10.606.10

Vanadium-containing Chloroperoxidase, domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Vanadium-containing Chloroperoxidase, domain 2
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Bromide peroxidase. [EC: 1.11.1.18]
RH + HBr + H(2)O(2) = RBr + 2 H(2)O.
  • Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate.
  • They catalyze the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds.
  • Bromoperoxidases also oxidize iodides.
 3 O81959 P81701 Q8LLW7
Chloride peroxidase. [EC: 1.11.1.10]
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.
 1 P49053