Linked Life Data

7016856

Source:http://linkedlifedata.com/resource/pubmed/id/7016856

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1981-8-10
pubmed:abstractText
The kinetic parameters describing the dissociation of GDP from the elongation factor Tu (EF-Tu) . GDP complex in the absence and presence of elongation factor Ts (EF-Ts) have been characterized using an equilibrium isotope exchange technique. The rate constant for dissociation of GDP from EF-tu was found to be 1.7 x 10(-3) s-1. Since this dissociation rate is greatly enhanced by EF-Ts, it follows that the dissociation of GDP in the presence of EF-Ts proceeds via the formation of a ternary EF-Tu . GDP . EF-Ts complex as represented below: EF-Tu . GDP + EF-Ts in equilibrium EF-Tu . GDP . EF-Ts in equilibrium EF-Tu . EF-Ts + GDP. Analysis of the exchange kinetics according to this reaction scheme yields a rate constant for the dissociation of GDP from the ternary complex of greater than or equal to 1270 s-1. The equilibrium association constants for GDP and EF-Ts to form the ternary complex was found to be 6.4 x 10(4) M-1 and 1.8 x 10(5) M-1, respectively. These results demonstrate that the dissociation of GDP from EF-Tu in the presence of EF-Ts is not the rate-limiting process in protein synthesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5591-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Kinetic studies on the interactions of Escherichia coli K12 elongation factor Tu with GDP and elongation factor Ts.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.