Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Microbiology & Fermentation Technology Regular Papers
Roles of a 20 kDa Protein Associated with a Carbocycle-Forming Enzyme Involved in Aminoglycoside Biosynthesis in Primary and Secondary Metabolism
Hideyuki TAMEGAIHiroshi SAWADAEriko NANGORie AOKIHaruka HIRAKAWATeruhiko IINOTadashi EGUCHI
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2010 Volume 74 Issue 6 Pages 1215-1219

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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 20 kDa 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 40 kDa 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.

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© 2010 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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