Interaction of glycyl-L-phenylalanine with escherichia coli phenylalanyl-tRNA synthetase

Sidney Hecht, S. D. Hawrelak

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The interaction of glycyl-L-phenylalanine with the phenylalanyl-tRNA synthetase from Escherichia coli has been studied by the attempted enzymatic acylation of tRNA with the dipeptide and with the dipeptidyl-AMP anhydride. Also measured were inhibition of the formation of phenylalanyl-tRNAPhe in the presence of glycyl-L-phenylalanine and the dipeptidyl-AMP analog, glycyl-L-phenylalan-inol-AMP, as well as the inhibition of ATP-PPi exchange in the presence of certain amino alcohol-AMP analogs of aminoacyl adenylates. The results, which indicated specific recognition of the dipeptide and dipeptidyl-AMP anhydride by the phenylalanyl-tRNA synthetase, are of interest in terms of the mechanism by which preexisting proteins are excluded from incorporation onto tRNA.

Original languageEnglish (US)
Pages (from-to)4967-4975
Number of pages9
JournalBiochemistry
Volume13
Issue number24
StatePublished - 1974
Externally publishedYes

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glycylphenylalanine
Phenylalanine-tRNA Ligase
Adenosine Monophosphate
Escherichia coli
Dipeptides
Transfer RNA
Anhydrides
RNA, Transfer, Phe
Amino Alcohols
Acylation
Transfer RNA Aminoacylation
Adenosine Triphosphate
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Interaction of glycyl-L-phenylalanine with escherichia coli phenylalanyl-tRNA synthetase. / Hecht, Sidney; Hawrelak, S. D.

In: Biochemistry, Vol. 13, No. 24, 1974, p. 4967-4975.

Research output: Contribution to journalArticle

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