Linked Life Data

2515292

Source:http://linkedlifedata.com/resource/pubmed/id/2515292

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-3-9
pubmed:abstractText
Glutathione peroxidase and glutathione S-transferase both utilize glutathione (GSH) to destroy organic hydroperoxides, and these enzymes are thought to serve an antioxidant function in mammalian cells by catalyzing the destruction of lipid hydroperoxides. Only two groups of procaryotes, the purple bacteria and the cyanobacteria, produce GSH, and we show in the present work that representatives from these two groups (Escherichia coli, Beneckea alginolytica, Rhodospirillum rubrum, Chromatium vinosum, and Anabaena sp. strain 7119) lack significant glutathione peroxidase and glutathione S-transferase activities. This finding, coupled with the general absence of polyunsaturated fatty acids in procaryotes, suggests that GSH-dependent peroxidases evolved in eucaryotes in response to the need to protect against polyunsaturated fatty acid oxidation. A second antioxidant function of GSH is mediated by glutathione thioltransferase, which catalyzes the reduction of various cellular disulfides by GSH. Two of the five GSH-producing bacteria studied (E. coli and B. alginolytica) produced higher levels of glutathione thioltransferase than found in rat liver, whereas the activity was absent in the other three species studied. The halobacteria produce gamma-glutamylcysteine rather than GSH, and assays for gamma-glutamylcysteine-dependent enzymes demonstrated an absence of peroxidase and S-transferase activities but the presence of significant thioltransferase activity. Based upon these results it appears that GSH and gamma-glutamylcysteine do not function in bacteria as antioxidants directed against organic hydroperoxides but do play a significant, although not universal, role in maintaining disulfides in a reduced state.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2844
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
429-35
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Evolution of antioxidant mechanisms: thiol-dependent peroxidases and thioltransferase among procaryotes.
pubmed:affiliation
Department of Chemistry, University of California-San Diego, La Jolla 92093-0506.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.