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CATH Superfamily 1.10.640.10

Haem peroxidase domain superfamily, animal type

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Haem peroxidase domain superfamily, animal type
".

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.
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FunFam 1: Peroxidasin homolog

There are 3 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
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 19 A0A1U7Q256 A0A1U7Q256 A1KZ92 A4IGL7 A5JUY8 A8WQH2 D2NUH5 D2NUH5 P11678 P22079
    (9 more...)
    Iodide peroxidase. [EC: 1.11.1.8]
    (1) 2 iodide + H(2)O(2) + 2 H(+) = diiodine + 2 H(2)O. (2) [Thyroglobulin]-L-tyrosine + iodide + H(2)O(2) = [thyroglobulin]-3- iodo-L-tyrosine + 2 H(2)O. (3) [Thyroglobulin]-3-iodo-L-tyrosine + iodide + H(2)O(2) = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H(2)O. (4) 2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H(2)O(2) = [thyroglobulin]- L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H(2)O. (5) [Thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L- tyrosine + H(2)O(2) = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H(2)O.
    • Thyroid peroxidase catalyzes the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine.
    • It catalyzes both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.
    		 5 P07202 P09933 P14650 P35419 Q8HYB7
    Myeloperoxidase. [EC: 1.11.2.2]
    Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O.
    • Is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal.
    • It differs from EC 1.11.1.10 in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8).
    • Hypochlorite in turn forms a number of antimicrobial products (Cl(2), chloramines, hydroxyl radical, singlet oxygen).
    • MPO also oxidizes bromide, iodide and thiocyanate.
    • In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
    		 2 P05164 P11247
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