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CATH Superfamily 1.10.420.10

Peroxidase, 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:

"
Peroxidase, 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 7 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
Catalase peroxidase. [EC: 1.11.1.21]
(1) Donor + H(2)O(2) = oxidized donor + 2 H(2)O. (2) 2 H(2)O(2) = O(2) + 2 H(2)O.
  • Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H(2)O(2) as donor, releasing O(2); both activities use the same heme active site.
  • In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
 1305 A0A023Z5R4 A0A023Z5R4 A0A025C7J2 A0A025C7J2 A0A026URM2 A0A026URM2 A0A027Z5Z4 A0A027Z5Z4 A0A027ZBL5 A0A027ZBL5
(1295 more...)
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 173 A0A178U798 A0A178UAR8 A0A178UJR4 A0A178UMG0 A0A178UNC2 A0A178UPS4 A0A178USM8 A0A178UVF1 A0A178V0D0 A0A178V1L7
    (163 more...)
    L-ascorbate peroxidase. [EC: 1.11.1.11]
    2 L-ascorbate + H(2)O(2) + 2 H(+) = L-ascorbate + L-dehydroascorbate + 2 H(2)O.
    • Oxidizes ascorbate and low molecular weight aromatic substrates.
    • The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 or undergoes non-enzymatic disproportionation to ascorbate and dehydroascorbate.
    		 37 A0A0D3H2X3 A0A0D9Z5N3 A0A0E0AYK7 A0A0E0EGI7 A0A0E0G839 A0A0E0IFH6 A0A0E0NGB2 A0A0E0P643 A0A0E0QM34 A0A178V282
    (27 more...)
    Cytochrome-c peroxidase. [EC: 1.11.1.5]
    2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.
      		 24 A0A0B0DM11 A0A0J5SCY2 A0A1D8NPB3 A0A1H6Q8P6 A0A1I9EY47 A0A229W615 A0A2H3GAG6 A4QVH4 C4YQ18 P00431
      (14 more...)
      Lignin peroxidase. [EC: 1.11.1.14]
      (1) 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O. (2) 2 (3,4-dimethoxyphenyl)methanol + H(2)O(2) = 2 (3,4- dimethoxyphenyl)methanol radical + 2 H(2)O.
      • Involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi.
      • The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (Fe(IV)=O radical cation) at the active site.
      • A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (Fe(IV)=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state.
      • The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously.
      • The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic beta-O-4 linked arylglycerol beta- aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site.
      • However larger lignin molecules can be degraded in the presence of veratryl alcohol.
      • It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates.
      • In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III).
      • This form can be rescued by interaction with two molecules of the free radical products.
      • In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
      		 12 P06181 P11542 P11543 P20010 P20013 P21764 P31837 P31838 P49012 P50622
      (2 more...)
      Manganese peroxidase. [EC: 1.11.1.13]
      2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O.
      • The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin.
      • The enzyme oxidizes a bound Mn(2+) ion to Mn(3+) in the presence of hydrogen peroxide.
      • The product, Mn(3+), is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn(2+) and insoluble Mn(4+).
      • The complexed Mn(3+) ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates.
      • It is inactive with veratryl alcohol or nonphenolic substrates.
      		 5 P19136 P78733 Q02567 Q70LM3 Q96TS6
      Versatile peroxidase. [EC: 1.11.1.16]
      (1) 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O. (2) 2 manganese(II) + 2 H(+) + H(2)O(2) = 2 manganese(III) + 2 H(2)O.
      • This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13 and EC 1.11.1.14.
      • Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates.
      		 3 O94753 Q9UR19 Q9UVP6