Editing Peroxidase (section)

==Characterization==
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|Gpx1]], [[GPX2 (gene)|Gpx2]], Gpx3, and [[GPX4|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.<ref>{{cite journal | vauthors = Atamna H, Boyle K | title = Amyloid-beta peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 103 | issue = 9 | pages = 3381–6 | date = Feb 2006 | pmid = 16492752 | pmc = 1413946 | doi = 10.1073/pnas.0600134103 | doi-access = free | bibcode = 2006PNAS..103.3381A }}</ref>

A typical group of peroxidases are the [[haloperoxidase]]s. This group is able to form reactive halogen species and, as a result, natural organohalogen substances.

A majority of peroxidase protein sequences can be found in the [[PeroxiBase]] database.