Identification and characterization of a novel l-amino acid ligase from Photorhabdus luminescens subsp. laumondii TT01

Kuniki Kino, Atsushi Noguchi, Toshinobu Arai, Makoto Yagasaki

    Research output: Contribution to journalArticle

    9 Citations (Scopus)

    Abstract

    l-Amino acid ligase catalyzes dipeptide synthesis from unprotected l-amino acids in an ATP-dependent manner. We recently identified a new member of l-amino acid ligase, the plu1440 protein, from Photorhabdus luminescens subsp. laumondii TT01 by in silico analysis. This protein was found to synthesize dipeptides containing l-asparagine at the N-terminus, which is a novel substrate specificity.

    Original languageEnglish
    Pages (from-to)39-41
    Number of pages3
    JournalJournal of Bioscience and Bioengineering
    Volume110
    Issue number1
    DOIs
    Publication statusPublished - 2010 Jul

    Fingerprint

    Photorhabdus
    Ligases
    Amino acids
    Dipeptides
    Amino Acids
    Proteins
    Asparagine
    Adenosinetriphosphate
    Substrate Specificity
    Computer Simulation
    Adenosine Triphosphate
    Substrates

    Keywords

    • Dipeptide
    • Enzymatic peptide synthesis
    • In silico screening
    • l-Amino acid ligase
    • Photorhabdus luminescens

    ASJC Scopus subject areas

    • Biotechnology
    • Applied Microbiology and Biotechnology
    • Bioengineering

    Cite this

    Identification and characterization of a novel l-amino acid ligase from Photorhabdus luminescens subsp. laumondii TT01. / Kino, Kuniki; Noguchi, Atsushi; Arai, Toshinobu; Yagasaki, Makoto.

    In: Journal of Bioscience and Bioengineering, Vol. 110, No. 1, 07.2010, p. 39-41.

    Research output: Contribution to journalArticle

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