Adaptability of nonnatural aromatic amino acids to the active center of the E. coli ribosomal A site.
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.
Hohsaka
T
T
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Sato
K
K
Sisido
M
M
Takai
K
K
Yokoyama
S
S
D000409:Alanine / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D001426:Bacterial Proteins / Q000096:biosynthesis; D001555:Benzene Derivatives / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D004926:Escherichia coli / Q000187:drug effects* / Q000378:metabolism; D015394:Molecular Structure; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D011500:Protein Synthesis Inhibitors / Q000378:metabolism / Q000494:pharmacology*; D011691:Puromycin / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D001555:Benzene Derivatives; D011500:Protein Synthesis Inhibitors; D010649:Phenylalanine; D011691:Puromycin; D000409:Alanine