Roles of a 20 kDa protein associated with a carbocycle-forming enzyme involved in aminoglycoside biosynthesis in primary and secondary metabolism

Hideyuki Tamegai, Hiroshi Sawada, Eriko Nango, Rie Aoki, Haruka Hirakawa, Teruhiko Iino, Tadashi Eguchi

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

2-Deoxy-.scyllo-inosose (DOI) synthase participates in the biosynthesis of 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics. The enzyme is expected to be of industrial use, because it converts a sustainable resource (glucose 6-phosphate) into carbocycle (DOI), which easily aromatizes to yield catechol. In the present study, we clarified the physiological role of a non- catalytic 20kDa protein, BtrC2, associated with DOI synthase from the butirosin-producer Bacillus circulans. Based on the results of complementation analysis using btrC2 disruptant and western analysis against catalytic 40kDa protein (BtrC) and BtrC2, it is suggested that BtrC2 has two functions. It is involved in the vitamin B6 biosynthesis in primary metabolism, like homologous protein (Pdx2) in Bacillus subtilis. Additionally, it takes part in butirosin biosynthesis as stabilizer of DOI synthase by forming a heterodimer with BtrC, and qualifies B. circulans for stable and constant production of butirosin for long periods.

Original languageEnglish
Pages (from-to)1215-1219
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Volume74
Issue number6
DOIs
Publication statusPublished - 2010
Externally publishedYes

Keywords

  • 2-deoxy-scyllo-inosose synthase
  • Antibiotic biosyntesis
  • Non-catalytic associated protein
  • Two functions
  • Vitamin B, biosynthesis

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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