Nanaomycin D reductase

Nanaomycin D reductase is a "flavoprotein enzyme" with a molecular weight of approximately 68,000 Da, containing FAD as a prosthetic group[1][2]. It catalyzes the reduction of nanaomycin D to nanaomycin A in the presence of NADH and under anaerobic conditions, forming part of the biosynthetic pathway for the antifungal antibiotic nanaomycin A in *Streptomyces rosa* var. *notoensis*[1][2][3]. The enzyme acts on various benzoisochromane-quinone antibiotics with substrate specificity, and functions mechanistically as an NADH-dependent quinone oxidoreductase[1][2][3]. Additional details: - The biosynthetic sequence involving nanaomycin D reductase proceeds as: "nanaomycin D → nanaomycin A → nanaomycin E → nanaomycin B"[1][2]. - Optimal activity occurs at pH 5.0 and 37°C (bacterial context)[1][2]. - The enzyme is "inhibited" by 1 mM Cu²⁺ and high concentrations of NADH (>50 µM)[1][2]. - Related biosynthetic enzymes (isochromanequinone reductases) have similar activities in other Streptomyces species[5]. - There is no evidence it functions as a receptor, transporter, or transcription factor. It is not a human drug target nor associated with drug interactions or safety concerns in clinical use. If you need structured identifiers (e.g., EC numbers), refer to quinone reductases (Oxidoreductases, EC 1.6.5.x). Nanaomycin D reductase is most accurately described as an NADH-dependent oxidoreductase involved in Streptomyces antibiotic biosynthesis[1][2][3][6].

Other names

Nanaomycin D:NADH oxidoreductaseQuinone reductase (in context of its activity)NADH dehydrogenase (quinone) (functional similarity; see [3])