Linked Life Data

18395526

Source:http://linkedlifedata.com/resource/pubmed/id/18395526

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2008-8-22
pubmed:abstractText
Trypanosomes and leishmania, the causative agents of several tropical diseases, possess a unique redox metabolism which is based on trypanothione. The bis(glutathionyl)spermidine is the central thiol that delivers electrons for the synthesis of DNA precursors, the detoxification of hydroperoxides and other trypanothione-dependent pathways. Many of the reactions are mediated by tryparedoxin, a distant member of the thioredoxin protein family. Trypanothione is kept reduced by the parasite-specific flavoenzyme trypanothione reductase. Since glutathione reductases and thioredoxin reductases are missing, the reaction catalyzed by trypanothione reductase represents the only connection between the NADPH- and the thiol-based redox metabolisms. Thus, cellular thiol redox homeostasis is maintained by the biosynthesis and reduction of trypanothione. Nearly all proteins of the parasite-specific trypanothione metabolism have proved to be essential.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1780
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1236-48
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism.
pubmed:affiliation
Biochemie-Zentrum der Universität Heidelberg, 69120 Heidelberg, Germany. luise.krauth-siegel@bzh.uni-heidelberg.de
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't