Differences in the Roles of a Glutamine Amidotransferase Subunit of Pyridoxal 5'-Phosphate Synthase betweenBacillus circulansandBacillus subtilis | Zendy

Shiori ITAGAKI | Zendy; Minami HAGA | Zendy; Yuji Oikawa | Zendy; Ayaka Sakoda | Zendy; Yoshie OHKE | Zendy; Hiroshi Sawada | Zendy; Tadashi Eguchi | Zendy; Hideyuki Tamegai | Zendy

Open Access

Differences in the Roles of a Glutamine Amidotransferase Subunit of Pyridoxal 5'-Phosphate Synthase betweenBacillus circulansandBacillus subtilis

Author(s) -

Shiori ITAGAKI,

Minami HAGA,

Yuji Oikawa,

Ayaka Sakoda,

Yoshie OHKE,

Hiroshi Sawada,

Tadashi Eguchi,

Hideyuki Tamegai

Publication year - 2013

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.130132

Subject(s) - glutamine amidotransferase , bacillus circulans , bacillus subtilis , biochemistry , pyridoxal , protein subunit , atp synthase , pyridoxal phosphate , biosynthesis , enzyme , glutamate synthase , complementation , acetolactate synthase , operon , chemistry , biology , glutamine , glutamine synthetase , bacteria , escherichia coli , genetics , cofactor , phenotype , gene , amino acid

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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