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Biosci Biotechnol Biochem. 2006 Nov;70(11):2790-2. Epub 2006 Nov 7.

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

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  • 1Department of Applied Chemistry, School of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo, Japan.

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 degrees 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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