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Concept
Peroxidase
Summary
Peroxidases or peroxide reductases (EC number 1.11.1.x) are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides.
Peroxidases typically catalyze a reaction of the form:
ROOR' + \overset{electron\atop donor}{2e^-} + 2H+ ->[\ce{Peroxidase}] {ROH} + R'OH
For many of these enzymes the optimal substrate is hydrogen peroxide, but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor in their active sites, or alternately redox-active cysteine or selenocysteine residues.
The nature of the electron donor is very dependent on the structure of the enzyme.
For example, horseradish peroxidase can use a variety of organic compounds as electron donors and acceptors. Horseradish peroxidase has an accessible active site, and many compounds can reach the site of the reaction.
On the other hand, for an enzyme such as cytochrome c peroxidase, the compounds that donate electrons are very specific, due to a very narrow active site.
Protein families that serve as peroxidases include:
Haem-using
haem peroxidase and the related animal heme-dependent peroxidases
DyP-type peroxidase family
Catalase
some haloperoxidase
Di-haem cytochrome c peroxidase
Non-heme
Thiol: glutathione peroxidase, peroxiredoxin
vanadium bromoperoxidase
Alkyl hydroperoxide reductase
Manganese peroxidase
NADH peroxidase
The glutathione peroxidase family consists of 8 known human isoforms. Glutathione peroxidases use glutathione as an electron donor and are active with both hydrogen peroxide and organic hydroperoxide substrates. Gpx1, Gpx2, Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, whereas Gpx6 is a selenoprotein in humans with cysteine-containing homologues in rodents.
Amyloid beta, when bound to heme, has been shown to have peroxidase activity.
A typical group of peroxidases are the haloperoxidases. This group is able to form reactive halogen species and, as a result, natural organohalogen substances.
Official source
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