D-amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity

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    12 Citations (Scopus)

    Abstract

    D-Alanine-D-alanine ligase (Ddl) is an important enzyme in the synthesis of bacterial peptidoglycan. The genes encoding Ddls from Escherichia coli K12 (EcDdlB), Oceanobacillus iheyensis JCM 11309 (OiDdl), Synechocystis sp. PCC 6803 (SsDdl) and Thermotoga maritima ATCC 43589 (TmDdl), the genomic DNA sequences of which have been determined, were cloned and the substrate specificities of these recombinant Ddls were investigated. Although OiDdl had a high substrate specificity for D-alanine; EcDdlB, SsDdl and TmDdl showed broad substrate specificities for D-serine, D-threonine, D-cysteine and glycine, in addition to D-alanine. Four D-amino acid dipeptides were produced using EcDdlB, and D-amino acid homo-dipeptides were successfully produced at high yields except for D-threonyl-D-threonine.

    Original languageEnglish
    Pages (from-to)623-628
    Number of pages6
    JournalJournal of Bioscience and Bioengineering
    Volume99
    Issue number6
    DOIs
    Publication statusPublished - 2005

    Fingerprint

    Dipeptides
    Substrate Specificity
    Amino acids
    Threonine
    Amino Acids
    Alanine
    Substrates
    Thermotoga maritima
    Synechocystis
    Escherichia coli K12
    Gene encoding
    Peptidoglycan
    DNA sequences
    Glycine
    Serine
    Escherichia coli
    Cysteine
    Enzymes
    Genes
    D-alanylalanine synthetase

    Keywords

    • D-alanine-D-alanine ligase
    • D-amino acid dipeptide
    • Dipeptide production
    • Vancomycin-resistant enterococci

    ASJC Scopus subject areas

    • Biotechnology
    • Bioengineering

    Cite this

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    title = "D-amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity",
    abstract = "D-Alanine-D-alanine ligase (Ddl) is an important enzyme in the synthesis of bacterial peptidoglycan. The genes encoding Ddls from Escherichia coli K12 (EcDdlB), Oceanobacillus iheyensis JCM 11309 (OiDdl), Synechocystis sp. PCC 6803 (SsDdl) and Thermotoga maritima ATCC 43589 (TmDdl), the genomic DNA sequences of which have been determined, were cloned and the substrate specificities of these recombinant Ddls were investigated. Although OiDdl had a high substrate specificity for D-alanine; EcDdlB, SsDdl and TmDdl showed broad substrate specificities for D-serine, D-threonine, D-cysteine and glycine, in addition to D-alanine. Four D-amino acid dipeptides were produced using EcDdlB, and D-amino acid homo-dipeptides were successfully produced at high yields except for D-threonyl-D-threonine.",
    keywords = "D-alanine-D-alanine ligase, D-amino acid dipeptide, Dipeptide production, Vancomycin-resistant enterococci",
    author = "Masaru Sato and Kotaro Kirimura and Kuniki Kino",
    year = "2005",
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    language = "English",
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    T1 - D-amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity

    AU - Sato, Masaru

    AU - Kirimura, Kotaro

    AU - Kino, Kuniki

    PY - 2005

    Y1 - 2005

    N2 - D-Alanine-D-alanine ligase (Ddl) is an important enzyme in the synthesis of bacterial peptidoglycan. The genes encoding Ddls from Escherichia coli K12 (EcDdlB), Oceanobacillus iheyensis JCM 11309 (OiDdl), Synechocystis sp. PCC 6803 (SsDdl) and Thermotoga maritima ATCC 43589 (TmDdl), the genomic DNA sequences of which have been determined, were cloned and the substrate specificities of these recombinant Ddls were investigated. Although OiDdl had a high substrate specificity for D-alanine; EcDdlB, SsDdl and TmDdl showed broad substrate specificities for D-serine, D-threonine, D-cysteine and glycine, in addition to D-alanine. Four D-amino acid dipeptides were produced using EcDdlB, and D-amino acid homo-dipeptides were successfully produced at high yields except for D-threonyl-D-threonine.

    AB - D-Alanine-D-alanine ligase (Ddl) is an important enzyme in the synthesis of bacterial peptidoglycan. The genes encoding Ddls from Escherichia coli K12 (EcDdlB), Oceanobacillus iheyensis JCM 11309 (OiDdl), Synechocystis sp. PCC 6803 (SsDdl) and Thermotoga maritima ATCC 43589 (TmDdl), the genomic DNA sequences of which have been determined, were cloned and the substrate specificities of these recombinant Ddls were investigated. Although OiDdl had a high substrate specificity for D-alanine; EcDdlB, SsDdl and TmDdl showed broad substrate specificities for D-serine, D-threonine, D-cysteine and glycine, in addition to D-alanine. Four D-amino acid dipeptides were produced using EcDdlB, and D-amino acid homo-dipeptides were successfully produced at high yields except for D-threonyl-D-threonine.

    KW - D-alanine-D-alanine ligase

    KW - D-amino acid dipeptide

    KW - Dipeptide production

    KW - Vancomycin-resistant enterococci

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