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

This article has now been updated. Please use the final version.

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

Masaru SATO, Kohtaro KIRIMURA, Kuniki KINO

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Keywords: D-alanine-D-alanine ligase, thermophile, vancomycin-resistant enterococci, D-amino acid dipeptide

JOURNAL FREE ACCESS Advance online publication

Article ID: 60307

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

The final version of this article is now available: Vol. 70 (2006) , No. 11 p.2790

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Abstract

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.

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