N-Tosyl-L-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tu from Escherichia coli.
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.
D000590:Amino Acid Chloromethyl Ketones / Q000494:pharmacology*; D002250:Carbon Radioisotopes; D003545:Cysteine; D004926:Escherichia coli / Q000235:genetics*; D006153:Guanosine Diphosphate / Q000378:metabolism; D007700:Kinetics; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism*; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology*
D000590:Amino Acid Chloromethyl Ketones; D002250:Carbon Radioisotopes; D010445:Peptide Elongation Factors; D006153:Guanosine Diphosphate; D014108:Tosylphenylalanyl Chloromethyl Ketone; D010444:Peptide Elongation Factor Tu; D003545:Cysteine