Esterification of Escherichia coli tRNAs with D-histidine and D-lysine by aminoacyl-tRNA synthetases.
It is generally believed that only L-amino acids are acceptable in protein synthesis, though some D-amino acids, including D-tyrosine, D-aspartate, and D-tryptophan are known to be bound enzymatically to tRNAs. In this report, we newly show that D-histidine and D-lysine are also able to be the substrates of respective Escherichia coli aminoacyl-tRNA synthetases.
Takayama
Toshimitsu
T
Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
Ogawa
Tetsuhiro
T
Hidaka
Makoto
M
Shimizu
Yoshihiro
Y
Ueda
Takuya
T
Masaki
Haruhiko
H
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D004951:Esterification; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism; D008239:Lysine / Q000737:chemistry* / Q000378:metabolism; D012329:RNA, Bacterial / Q000737:chemistry* / Q000378:metabolism; D012343:RNA, Transfer / Q000737:chemistry* / Q000378:metabolism; D013237:Stereoisomerism
D012329:RNA, Bacterial; D006639:Histidine; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases; D008239:Lysine