AI Article Synopsis
- The study focuses on the role of plant-derived aromatic substances in the growth of Streptomyces and investigates an enzyme that reduces specific chemical compounds in Streptomyces coelicolor A3(2).
- Researchers identified this enzyme as a product of the gene SCO2180, which shares similarities with a known enzyme involved in energy metabolism.
- The findings suggest that this enzyme forms a dimer and has a broader function in reducing quinonic substrates, indicating that similar enzymatic activities are present in various soil-dwelling Streptomyces strains.
Article Abstract
Metabolism and utilization of plant-derived aromatic substances are fundamental to the saprophytic growth of Streptomyces. Here, we studied an enzyme activity reducing 2,6-dichlorophenolindophenol and nitroblue tetrazolium in the culture supernatant of Streptomyces coelicolor A3(2). N-terminal amino acid sequencing of a nitroblue tetrazolium-reducing enzyme revealed that the enzyme corresponds to the SCO2180 product. The protein exhibited a marked similarity with dihydrolipoamide dehydrogenase, the E3 subunit of 2-oxo-acid dehydrogenase complex. A recombinant SCO2180 protein formed a homodimer and exhibited a diaphorase activity catalyzing NADH-dependent reduction of various quinonic substrates. Similar nitroblue tetrazolium-reducing activities were observed for other Streptomyces strains isolated from soil, implying that the diaphorase-catalyzed reduction of quinonic substances widely occurs in the extracytoplasmic space of Streptomyces.
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| http://dx.doi.org/10.1016/j.bbrc.2018.07.083 | DOI Listing |
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