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Adaptability of nonnatural aromatic amino acids to the active center of the E. coli ribosomal A site
Author(s) -
Hohsaka Takahiro,
Sato Ken,
Sisido Masahiko,
Takai Kazuyuki,
Yokoyama Shigeyuki
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80436-x
Subject(s) - puromycin , amino acid , ribosomal rna , escherichia coli , ribosomal protein , stereochemistry , chemistry , adaptability , aromatic amino acids , biochemistry , active site , biology , ribosome , protein biosynthesis , ecology , enzyme , rna , gene
3'‐ N ‐Aminoacyl analogs of puromycin with nonnatural aromatic amino acids were synthesized and their inhibitory activity in E.coli in vitro protein synthesizing system was evaluated. The analogs with l ‐2‐naphthylalanine, l ‐ p ‐biphenylalanine, l ‐2‐anthrylalanine and trans ‐ l ‐ p ‐phenylazophenylalanine were found to inhibit the protein synthesis with high efficiency. The inhibition suggests that these nonnatural amino acids are accepted by the active center of the E. coli ribosomal A site. A model for the adaptability of nonnatural aromatic amino acids to the active center is proposed.