N-Tosyl-L-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tu from Escherichia coli

FEBS Lett. 1982 Dec 27;150(2):485-8. doi: 10.1016/0014-5793(82)80795-3.

Abstract

Elongation factor EF-Tu from Escherichia coli was labelled with N-[14C]tosyl-L-phenylalanylchloromethane, digested with trypsin and the peptides obtained separated by HPLC. The only radioactive peak recovered corresponded to tryptic peptide containing residues 75-98. Sequencing of the peptide by automated Edman degradation identified cysteine 81 as the site of N-tosyl-L-phenylalanylchloromethane modification. These results confirm the importance of this residue for the interaction with aminoacyl-tRNAs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Chloromethyl Ketones / pharmacology*
  • Carbon Radioisotopes
  • Cysteine
  • Escherichia coli / genetics*
  • Guanosine Diphosphate / metabolism
  • Kinetics
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors / metabolism*
  • Tosylphenylalanyl Chloromethyl Ketone / pharmacology*

Substances

  • Amino Acid Chloromethyl Ketones
  • Carbon Radioisotopes
  • Peptide Elongation Factors
  • Guanosine Diphosphate
  • Tosylphenylalanyl Chloromethyl Ketone
  • Peptide Elongation Factor Tu
  • Cysteine