Differences in the Roles of a Glutamine Amidotransferase Subunit of Pyridoxal 5'-Phosphate Synthase between <i>Bacillus circulans</i> and <i>Bacillus subtilis</i>

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  • ITAGAKI Shiori
    Department of Correlative Study of Physics and Chemistry, Graduate School of Integrated Basic Sciences, Nihon University
  • HAGA Minami
    Department of Correlative Study of Physics and Chemistry, Graduate School of Integrated Basic Sciences, Nihon University
  • OIKAWA Yuji
    Department of Correlative Study of Physics and Chemistry, Graduate School of Integrated Basic Sciences, Nihon University
  • SAKODA Ayaka
    Department of Correlative Study of Physics and Chemistry, Graduate School of Integrated Basic Sciences, Nihon University
  • OHKE Yoshie
    Department of Chemistry, College of Humanities and Sciences, Nihon University
  • SAWADA Hiroshi
    Department of Correlative Study of Physics and Chemistry, Graduate School of Integrated Basic Sciences, Nihon University Department of General Studies, College of Humanities and Sciences, Nihon University
  • EGUCHI Tadashi
    Department of Chemistry and Materials Science, Graduate School of Science and Engineering, Tokyo Institute of Technology
  • TAMEGAI Hideyuki
    Department of Correlative Study of Physics and Chemistry, Graduate School of Integrated Basic Sciences, Nihon University Department of Chemistry, College of Humanities and Sciences, Nihon University

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  • Differences in the Roles of a Glutamine Amidotransferase Subunit of Pyridoxal 5'-Phosphate Synthase between Bacillus circulans and Bacillus subtilis

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Abstract

BtrC2 of the butirosin producer Bacillus circulans is a non-catalytic subunit of 2-deoxy-scyllo-inosose (DOI) synthase that is involved in butirosin biosynthesis, and also a homolog of glutamine amidotransferase subunit (PdxT) of pyridoxal 5'-phosphate (PLP) synthase of Bacillus subtilis. BtrC2 has been found to have functions in B. circulans both in primary and secondary metabolism. In this study, we investigated the properties of PdxT of B. subtilis in order to determine whether the property of enzyme stabilization is universal among PdxT homologs. Complementation with PdxT in the btrC2 disruptant of B. circulans restored the growth and short-term production of antibiotics, but long-term production of antibiotics cannot be restored. Additionally, PdxT did not bind physically with or stabilize BtrC. Our results indicate that the function of BtrC2 in secondary metabolism is specific properties, not universal among PdxT homologs.

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