Conformational activation of the yeast phenylalanyl-tRNA synthetase catalytic site induced by tRNAPhe interaction: triggering of adenosine or CpCpA trinucleoside diphosphate aminoacylation upon binding of tRNAPhe lacking these residues.

Adenosine or CpCpA trinucleoside diphosphate can be aminoacylated by phenylalanyl-tRNA synthetase [L-phenylalanine:tRNAPhe ligase (AMP forming), EC 6.1.1.20] when the reaction takes place in the presence of tRNAPhe deprived of its 3' adenosine or pCpCpA terminus. This shows that, upon interaction wi...

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出版年:	Proc Natl Acad Sci U S A
主要な著者:	Renaud, M, Bacha, H, Remy, P, Ebel, J P
フォーマット:	Artigo
言語:	Inglês
出版事項:	National Academy of Sciences 1981
主題:	Research Article
オンライン･アクセス:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC319180/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7015339/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.3.1606
タグ:	タグ追加タグなし, このレコードへの初めてのタグを付けませんか!

Conformational activation of the yeast phenylalanyl-tRNA synthetase catalytic site induced by tRNAPhe interaction: triggering of adenosine or CpCpA trinucleoside diphosphate aminoacylation upon binding of tRNAPhe lacking these residues.

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