Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1982-12-21
pubmed:abstractText
Thirteen different yeast tRNAPhe variants with single nucleotide changes in positions 34-37 in the anticodon region were prepared by an enzymatic procedure described previously. Aminoacylation kinetics using purified yeast phenylalanyl-tRNA synthetase revealed that the level of aminoacylation was very different for different sequences inserted. The low level of aminoacylation was the result of a steady state between a slow forward reaction rate and spontaneous deacylation of the product. Aminoacylation kinetics performed at higher synthetase concentrations revealed that substitution at position 34 in tRNAPhe decreased the Km nearly 10-fold but only had a small effect on Vmax. Similar substitutions at positions 35, 36, and 37 had a lesser effect. These data suggest a sequence-specific contact between the anticodon of yeast tRNAPhe and the cognate synthetase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3921-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Specific interaction of anticodon loop residues with yeast phenylalanyl-tRNA synthetase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.