PMID: 3771102Aug 1, 1986Paper

Dipeptide synthesis catalyzed by aminoacyl-tRNA synthetases from Bacillus stearothermophilus

International Journal of Peptide and Protein Research
H NakajimaK Imahori

Abstract

A new approach to enzymatic peptide synthesis by using aminoacyl-tRNA synthetase (ARS) as a catalyst has been investigated. Four ARSs (AspRS, HisRS, LeuRS and TyrRS) have been purified from a thermophilic bacterium, Bacillus stearothermophilus. By using TyrRS as a catalyst, tyrosine and leucinamide were shown to be condensed in the presence of ATP to give tyrosylleucinamide. In this manner, all of the ARSs investigated catalyzed the peptide synthesis reactions. TyrRS did not have strict specificity for the amino acid derivatives used as substrates and even D-amino acids were incorporated into peptides fairly easily in this enzymatic reaction. Preparative scale synthesis of L-Tyr-L-LeuNH2 was carried out and from this the scope and limitation of this new enzymatic reaction as a tool to the peptide synthesis has been described.

References

Jan 1, 1979·Methods in Enzymology·L L KisselevG K Kovaleva
Apr 1, 1968·Journal of Biochemistry·S KijimaK Imahori
Jun 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·R B LoftfieldH Jakubowski

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Citations

May 1, 1989·Biotechnology and Bioengineering·A FlörsheimerC Wandrey
Dec 1, 1991·Experientia·C H Wong, K T Wang
Aug 3, 1999·Biological Chemistry·W FreistJ G Arnez
Feb 15, 1996·Enzyme and Microbial Technology·I GillE N Vulfson
Jul 15, 1987·Biochemical and Biophysical Research Communications·S KitabatakeH Nakajima

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