Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum

Kuniki Kino, Yuji Nakazawa, Makoto Yagasaki

    研究成果: Article

    28 引用 (Scopus)

    抄録

    Despite its utility, dipeptides have not been widely used due to the absence of an efficient manufacturing method. Recently, a novel method for effective production of dipeptides using l-amino acid α-ligase (Lal) is presented. Lal, which is only identified in Bacillus subtilis, catalyzes dipeptide synthesis from unprotected amino acids in an ATP-dependent manner. However, not all the dipeptide can be synthesized by Lal from B. subtilis (BsLal) due to its substrate specificity. Here, we attempted to find a novel Lal exhibiting different substrate specificity from BsLal. By in silico screening based on the amino acid sequence of BsLal, RSp1486a an unknown protein from Ralstonia solanacearum was found to show the Lal activity. RSp1486a exhibited different substrate specificity from BsLal, and preferably synthesized hetero-dipeptides where more bulky amino acid was placed at N terminus and less bulky amino acid was placed at C terminus in opposition to those synthesized by BsLal.

    元の言語English
    ページ(範囲)536-540
    ページ数5
    ジャーナルBiochemical and Biophysical Research Communications
    371
    発行部数3
    DOI
    出版物ステータスPublished - 2008 7 4

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    Ralstonia solanacearum
    Dipeptides
    Ligases
    Amino Acids
    Substrate Specificity
    Bacillus subtilis
    Substrates
    Computer Simulation
    Bacilli
    Amino Acid Sequence
    Adenosine Triphosphate
    Screening

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

    これを引用

    Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum. / Kino, Kuniki; Nakazawa, Yuji; Yagasaki, Makoto.

    :: Biochemical and Biophysical Research Communications, 巻 371, 番号 3, 04.07.2008, p. 536-540.

    研究成果: Article

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