Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase

R. C. Scarpulla*, C. E. Deutch, R. L. Soffer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Leucyl, phenylalanyl-tRNA-protein transferase also catalyzes transfer of methionyl residues as indicated by (i) copurification over a 1000-fold range of transfer activities for all three amino acids and (ii) loss of methionyl transfer activity in a mutant of E. coli lacking the transferase and reappearance of this activity in a transferase revertant. The purified enzyme was found to use Met-tRNAmMet in preference to Met-tRNAfMet as donor substrate. Peptides containing a basic amino acid at the NH2-terminus functioned as acceptors for the transfer of methionyl residues.

Original languageEnglish (US)
Pages (from-to)584-589
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume71
Issue number2
DOIs
StatePublished - Jul 26 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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