Esterification of Eschericia coli tRNAs with D-histidine and D-lysine by aminoacyl-tRNA synthetases

Toshimitsu Takayama; Tetsuhiro Ogawa; Makoto Hidaka; Yoshihiro Shimizu; Takuya Ueda; Haruhiko Masaki

doi:10.1271/bbb.69.1040

Esterification of Eschericia coli tRNAs with D-histidine and D-lysine by aminoacyl-tRNA synthetases

Toshimitsu Takayama, Tetsuhiro Ogawa, Makoto Hidaka, Yoshihiro Shimizu, Takuya Ueda, Haruhiko Masaki^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1040-1041
Number of pages	2
Journal	Bioscience, Biotechnology and Biochemistry
Volume	69
Issue number	5
DOIs	https://doi.org/10.1271/bbb.69.1040
Publication status	Published - 2005 May
Externally published	Yes

Keywords

Aminoacyl-tRNA synthetase
D-amino acids

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

Access to Document

10.1271/bbb.69.1040

Cite this

@article{b04c17e379c5448199a3525800d0476a,

title = "Esterification of Eschericia coli tRNAs with D-histidine and D-lysine by aminoacyl-tRNA synthetases",

abstract = "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.",

keywords = "Aminoacyl-tRNA synthetase, D-amino acids",

author = "Toshimitsu Takayama and Tetsuhiro Ogawa and Makoto Hidaka and Yoshihiro Shimizu and Takuya Ueda and Haruhiko Masaki",

year = "2005",

month = may,

doi = "10.1271/bbb.69.1040",

language = "English",

volume = "69",

pages = "1040--1041",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "5",

}

TY - JOUR

T1 - Esterification of Eschericia coli tRNAs with D-histidine and D-lysine by aminoacyl-tRNA synthetases

AU - Takayama, Toshimitsu

AU - Ogawa, Tetsuhiro

AU - Hidaka, Makoto

AU - Shimizu, Yoshihiro

AU - Ueda, Takuya

AU - Masaki, Haruhiko

PY - 2005/5

Y1 - 2005/5

N2 - 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.

AB - 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.

KW - Aminoacyl-tRNA synthetase

KW - D-amino acids

UR - http://www.scopus.com/inward/record.url?scp=22444439579&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=22444439579&partnerID=8YFLogxK

U2 - 10.1271/bbb.69.1040

DO - 10.1271/bbb.69.1040

M3 - Article

C2 - 15914930

AN - SCOPUS:22444439579

SN - 0916-8451

VL - 69

SP - 1040

EP - 1041

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 5

ER -

Esterification of Eschericia coli tRNAs with D-histidine and D-lysine by aminoacyl-tRNA synthetases

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this