Substrate Specificity of ThermostableD-Alanine-D-alanine ligase fromThermotoga maritimaATCC 43589 | Zendy

Masaru Satô | Zendy; Kohtaro Kirimura | Zendy; Kuniki Kino | Zendy

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Substrate Specificity of ThermostableD-Alanine-D-alanine ligase fromThermotoga maritimaATCC 43589

Author(s) -

Masaru Satô,

Kohtaro Kirimura,

Kuniki Kino

Publication year - 2006

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.60307

Subject(s) - thermotoga maritima , thermostability , dna ligase , alanine , peptidoglycan , biochemistry , serine , biosynthesis , substrate (aquarium) , chemistry , biology , amino acid , cell wall , enzyme , escherichia coli , gene , ecology

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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