Non-standard amino acid recognition by Escherichia coli leucyl-tRNA synthetase.

S. A. Martinis, G. E. Fox

Research output: Contribution to journalArticlepeer-review


Recombinant E. coli leucyl-tRNA synthetase was screened for amino acid-dependent pyrophosphate exchange activity using noncognate aliphatic amino acids including norvaline, homocysteine, norleucine, methionine, and homoserine. [32P]-labeled reaction products were separated by thin layer chromatography using a novel solvent system and then quantified by phosphorimaging. Norvaline which differs from leucine by only one methyl group stimulated pyrophosphate exchange activity as did both homocysteine and norleucine to a lesser extent. The KM parameters for leucine and norvaline were measured to be 10 micromoles and 1.5 mM, respectively. Experiments are in progress to determine if norvaline is transferred to tRNA(Leu) and/or edited by a pre- or post-transfer mechanism.

Original languageEnglish (US)
Pages (from-to)125-128
Number of pages4
JournalNucleic acids symposium series
StatePublished - 1997
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)


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