Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2790-2792
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume70
Issue number11
DOIs
Publication statusPublished - 2006 Dec 1

    Fingerprint

Keywords

  • D-alanine-D-alanine ligase
  • D-amino acid dipeptide
  • Thermophile
  • Vancomycin-resistant enterococci

ASJC Scopus subject areas

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

Cite this