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

作者信息

Sato Masaru, Kirimura Kohtaro, Kino Kuniki

机构信息

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

出版信息

Biosci Biotechnol Biochem. 2006 Nov;70(11):2790-2. doi: 10.1271/bbb.60307. Epub 2006 Nov 7.

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.