Extracytoplasmic diaphorase activity of Streptomyces coelicolor A3(2).
Biochem Biophys Res Commun
; 503(3): 1581-1586, 2018 09 10.
Article
em En
| MEDLINE
| ID: mdl-30054046
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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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Citoplasma
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3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)
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Streptomyces coelicolor
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Di-Hidrolipoamida Desidrogenase
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2018
Tipo de documento:
Article