Linked Life Data

18084888

Source:http://linkedlifedata.com/resource/pubmed/id/18084888

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-12-18
pubmed:abstractText
Peroxiredoxins compose a superfamily of peroxidases ubiquitously found throughout evolution in prokaryotes, archaea and eukaryotes. These enzymes contain a conserved catalytic peroxidatic cysteine (Cp) in the N-terminal region of the protein. The residues surrounding Cp and the catalytic site appear also to be well conserved. Peroxiredoxins can be classified either into three subfamilies according to their catalytic mechanism or into five subfamilies according to sequence homology. Notably, the number of peroxiredoxin genes increased during evolution. In eukaryotes, the higher number of genes coding for peroxiredoxin family members is due to the existence of different isoforms targeted to different subcellular compartments but is probably due also to the acquisition of new functions. Indeed, it has been postulated that the antioxidant protective role of peroxiredoxins, which is particularly critical in prokaryotes, in yeasts and in parasitic eukaryotes, may have evolved to a modulatory role in hydrogen peroxide signaling in plants and animals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0306-0225
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-40
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Evolution of the peroxiredoxins.
pubmed:affiliation
Laboratory of Cell Biology, Institut des Sciences de la Vie, Université catholique de Louvain, Louvain-la-Neuve, Belgium.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't