Linked Life Data

7070377

Source:http://linkedlifedata.com/resource/pubmed/id/7070377

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-6-21
pubmed:abstractText
It is shown for beef pancreas tryptophanyl-tRNA synthetase that there exists a mechanism which provides additional discrimination in vitro after misactivation of monofluorinated tryptophan analogs. In the presence of tryptophan one can observe a rapid decomposition of noncognate aminoacyl adenylate-enzyme complexes containing 4-fluoro-, 6-fluoro- or 7-fluorotryptophan residues, whereas the stoichiometry aminoacyl adenylate.enzyme complexes with tryptophan and 4-fluorotryptophan residues is not changed. Rejection of noncognate aminoacyl adenylate-enzyme complexes is connected neither with the enzymatic hydrolysis of aminoacyl adenylate nor with the competition of non-cognate aminoacyl adenylate and the added amino acid for the enzyme binding site. Rejection of noncognate complexes is presumably caused by the interaction between the active centers localized on two subunits, with one of them being occupied by an amino acid molecule and the other one by noncognate aminoacyl adenylate.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
170-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Increasing specificity of tryptophanyl-tRNA synthetase after amino acid activation].
pubmed:publicationType
Journal Article, English Abstract