Substrate Specificity of Thermostable <small>D</small>-Alanine-<small>D</small>-alanine ligase from Thermotoga maritima ATCC 43589

Masaru SATO; Kohtaro KIRIMURA; Kuniki KINO

doi:10.1271/bbb.60307

Biochemistry & Molecular Biology Notes

Substrate Specificity of Thermostable D-Alanine-D-alanine ligase from Thermotoga maritima ATCC 43589

Masaru SATO, Kohtaro KIRIMURA, Kuniki KINO

著者情報

キーワード: D-alanine-D-alanine ligase, thermophile, vancomycin-resistant enterococci, D-amino acid dipeptide

ジャーナルフリー

2006 年 70 巻 11 号 p. 2790-2792

DOI https://doi.org/10.1271/bbb.60307

View "Advance Publication" version (November 7, 2006).

詳細

抄録

D-Alanine-D-alanine ligase (Ddl) and its mutants maintain the biosynthesis of peptidoglycan, and the substrate specificity of Ddls partially affects the resistance mechanism of vancomycin-resistant enterococci. Through investigation of Ddls, Ddl from Thermotoga maritima ATCC 43589 showed novel characteristics, vis. thermostability up to 90 °C and broad substrate specificity toward 15 D-amino acids, particularly D-alanine, D-cysteine, and D-serine, in that order.

責任著者(Corresponding author)

J-STAGEへの登録はこちら（無料）