title: Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589.
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.
authors.affiliation: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo, Japan.
authors.forename: Masaru
authors.initials: M
authors.lastname: Sato
authors.forename: Kohtaro
authors.initials: K
authors.lastname: Kirimura
authors.forename: Kuniki
authors.initials: K
authors.lastname: Kino
mesh_terms: D004795:Enzyme Stability; D010453:Peptide Synthases / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D013379:Substrate Specificity; D013696:Temperature; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics
chemical_list: D010453:Peptide Synthases; C019638:D-alanylalanine synthetase