Two groups of thermophilic amino acid aminotransferases exhibiting broad substrate specificities for the synthesis of phenylglycine derivatives

Daisuke Koma, Toshiya Sawai, Ryotaro Hara, Shigeaki Harayama, Kuniki Kino

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    Thirty two thermophilic amino acid aminotransferases (AATs) were expressed in Escherichia coli as soluble and active proteins. Based on their primary structures, the 32 AATs were divided into four phylogenetic groups (classes I, II, IV, and V). The substrate specificities of these AATs were examined, and 12 AATs were found capable of synthesizing ring-substituted phenylglycine derivatives such as hydroxyl-, methoxy-, and fluorophenylglycines. Eleven out of the 12 AATs were enzymes belonging to two phylogenetic groups namely, one subgroup of the class I family and the class IV family. AATs in these two groups may thus be useful for the synthesis of a variety of ring-substituted phenylglycine derivatives.

    Original languageEnglish
    Pages (from-to)775-784
    Number of pages10
    JournalApplied Microbiology and Biotechnology
    Volume79
    Issue number5
    DOIs
    Publication statusPublished - 2008 Jul

    Fingerprint

    Substrate Specificity
    Transaminases
    Amino acids
    Derivatives
    Amino Acids
    Acids
    Substrates
    Escherichia coli
    Hydroxyl Radical
    Enzymes
    Proteins

    Keywords

    • Aminotransferase
    • Nonproteinogenic amino acid
    • Phenylglycine
    • Thermophile
    • Unnatural amino acid

    ASJC Scopus subject areas

    • Biotechnology
    • Microbiology
    • Bioengineering
    • Microbiology (medical)

    Cite this

    Two groups of thermophilic amino acid aminotransferases exhibiting broad substrate specificities for the synthesis of phenylglycine derivatives. / Koma, Daisuke; Sawai, Toshiya; Hara, Ryotaro; Harayama, Shigeaki; Kino, Kuniki.

    In: Applied Microbiology and Biotechnology, Vol. 79, No. 5, 07.2008, p. 775-784.

    Research output: Contribution to journalArticle

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