Interaction between phenylalanine-tRNA and the allosteric first enzyme of the aromatic amino acid biosynthetic pathway

E. Duda, M. Staub, P. Venetianer, G. Dénes

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The experiments described in this report demonstrate that the first /allosteric/ enzyme of the common pathway of the aromatic amino acid biosynthesis, the phenyl-alanine-sensitive DAHP-synthase strongly and specifically binds phenylalanyl-tRNA, either charged with amino acid, or uncharged. A complex of charged tRNA with the allosteric enzyme would be a likely candidate for the role of the repressor in this system. Work is in progress to investigate this possibility.

Original languageEnglish
Pages (from-to)992-997
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume32
Issue number6
Publication statusPublished - Sep 30 1968

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Aromatic Amino Acids
Biosynthetic Pathways
Transfer RNA
Phenylalanine
3-Deoxy-7-Phosphoheptulonate Synthase
Biosynthesis
Enzymes
Alanine
Amino Acids
Experiments

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Interaction between phenylalanine-tRNA and the allosteric first enzyme of the aromatic amino acid biosynthetic pathway. / Duda, E.; Staub, M.; Venetianer, P.; Dénes, G.

In: Biochemical and Biophysical Research Communications, Vol. 32, No. 6, 30.09.1968, p. 992-997.

Research output: Contribution to journalArticle

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