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

FEBS Letters

Rychlík, Ivan²  Clark, Brian F.C.³  Jonák, Jiří²  Petersen, Torben E.¹ 

[1] Department of Molecular Biology, Aarhus University, C.F Møllers Allè 130, DK-8000 Aarhus C Denmark;Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Flemingovo n. 2, 16637 Prague 6, Czechoslovakia;Department of Chemistry, Aarhus University, Langelandsgade 140, DK-8000 Aarhus C, Denmark

关键词: Elongation factor EF-Tu;    Cysteine 81;    Escherichia coli;    Modification by TPCK;    HPLC chromatography;    Tryptic peptide;    TPCK;    N-tosyl-L-phenylalanylchloro-methane or L-1-tosylamido-2-phenylethyl chloromethyl ketone;    EF-Tu;    elongation factor Tu;    HPLC;    high-performance liquid chromatography;    PTH;    phenylthio-hydantoine;   

DOI  :  10.1016/0014-5793(82)80795-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown