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

    Fingerprint

    Thermotoga maritima
    substrate specificity
    Substrate Specificity
    ligases
    alanine
    Peptidoglycan
    Biosynthesis
    Substrates
    Vancomycin
    Alanine
    Serine
    Cysteine
    Amino acids
    Amino Acids
    vancomycin
    peptidoglycans
    Enterococcus
    thermal stability
    resistance mechanisms
    serine

    Keywords

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

    ASJC Scopus subject areas

    • Bioengineering
    • Biotechnology
    • Biochemistry
    • Biochemistry, Genetics and Molecular Biology(all)
    • Chemistry (miscellaneous)
    • Applied Microbiology and Biotechnology
    • Food Science

    Cite this

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    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°C and broad substrate specificity toward 15 D-amino acids, particularly D-alanine, D-cysteine, and D-serine, in that order.",
    keywords = "D-alanine-D-alanine ligase, D-amino acid dipeptide, Thermophile, Vancomycin-resistant enterococci",
    author = "Masaru Sato and Kotaro Kirimura and Kuniki Kino",
    year = "2006",
    doi = "10.1271/bbb.60307",
    language = "English",
    volume = "70",
    pages = "2790--2792",
    journal = "Bioscience, Biotechnology and Biochemistry",
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    publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
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    TY - JOUR

    T1 - Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589

    AU - Sato, Masaru

    AU - Kirimura, Kotaro

    AU - Kino, Kuniki

    PY - 2006

    Y1 - 2006

    N2 - 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.

    AB - 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.

    KW - D-alanine-D-alanine ligase

    KW - D-amino acid dipeptide

    KW - Thermophile

    KW - Vancomycin-resistant enterococci

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