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

Shiori ITAGAKI; Minami HAGA; Yuji OIKAWA; Ayaka SAKODA; Yoshie OHKE; Hiroshi SAWADA; Tadashi EGUCHI; Hideyuki TAMEGAI

doi:10.1271/bbb.130132

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

Shiori ITAGAKI, Minami HAGA, Yuji OIKAWA, Ayaka SAKODA, Yoshie OHKE, Hiroshi SAWADA, Tadashi EGUCHI, Hideyuki TAMEGAI

著者情報

キーワード: 2-deoxy-scyllo-inosose synthase, BtrC2, dual functions, pyridoxal 5'-phosphate biosynthesis, enzyme stabilization

ジャーナルフリー早期公開

論文ID: 130132

DOI https://doi.org/10.1271/bbb.130132

この記事には本公開記事があります。

The final version of this article is now available: Vol. 77 (2013) , No. 7 p.1481

詳細

抄録

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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