Linked Life Data

19362171

Source:http://linkedlifedata.com/resource/pubmed/id/19362171

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2009-6-15
pubmed:abstractText
Thioredoxin (Trx) and glutathione/glutaredoxin (GSH/Grx) systems play the dominant role in cellular redox homeostasis. Recently the Trx system has been shown to be responsible to control the balance of GSH/GSSG once the glutathione reductase system is not available. To decipher the structural basis of electron transfer from the Trx system to GSSG, we solved the crystal structures of oxidized Trx1 and glutathionylated Trx1Cys33Ser mutant at 1.76 and 1.80 A, respectively. Comparative structural analysis revealed a key residue Met35 involved in the Trx-GSSG recognition. Subsequent mutagenesis and kinetic studies proved that Met35Arg mutation could alter the apparent K(m) and V(max) values of the reaction. These findings gave us the structural insights into GSSG reduction catalyzed by the Trx system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1794
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1218-23
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system.
pubmed:affiliation
Institute of Protein Research, Tongji University, Shanghai, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't