Linked Life Data

3350808

Source:http://linkedlifedata.com/resource/pubmed/id/3350808

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1988-5-2
pubmed:abstractText
The release of a chromophoric analogue of GDP, 2-amino-6-mercaptopurine riboside 5'-diphosphate (thioGDP), from its complex with elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). The mechanism of this reaction includes a ternary complex; EF-Tu.thioGDP.EF-Ts (Eccleston, J. F. (1984) J. Biol. Chem. 259, 12997-13003). This mechanism has been further investigated using pressure relaxation techniques combined with spectrophotometric measurements. The equilibrium of a solution of EF-Tu, EF-Ts, and thioGDP over a range of concentrations is perturbed on increasing the pressure to 150 atm. Rapid decrease of the pressure back to 1 atm results in a biphasic relaxation process, an initial fast phase which is complete within 1 ms followed by a slower phase. This is interpreted as the result of an isomerization of the EF-Tu.thioGDP.EF-Ts ternary complex which occurs before the release of thioGDP. Such an isomerization process may be a general feature in the release of GDP from guanosine nucleotide-binding proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4668-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
The kinetic mechanism of the release of nucleotide from elongation factor Tu promoted by elongation factor Ts determined by pressure relaxation studies.
pubmed:affiliation
National Institute for Medical Research, Mill Hill, London, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't