OXYGEN-INSENSITIVE NITROFURAN REDUCTASES IN SALMONELLA TYPHIMURIUM TA100

  • TATSUMI KIYOSHI
    Present address Institute of Pharmaceutical Sciences, Hiroshima University School of Medicine
  • DOI TAKAYOSHI
    Present address Central Research Division, Takeda Chemical Industries, Ltd.
  • YOSHIMURA HIDETOSHI
    Faculty of Pharmaceutical Sciences, Kyushu University
  • KOGA HIDEO
    Faculty of Pharmaceutical Sciences, Kyushu University
  • HORIUCHI TADAO
    Faculty of Pharmaceutical Sciences, Kyushu University

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The present study demonstrated by DEAE-cellulose column chromatography that oxygen-insensitive nitrofuran reductases in Salmonella typhimurium TA100 consisted of at least two reductases, NADPH-and NAD (P) H-linked enzymes. The NADPH-and NADH-linked activities of the latter enzyme seemed to originate from a single enzyme, because both activities were similarly inactivated by heat and urea treatments, and also inhibited by dicumarol. On the other hand, the NADPH-linked enzyme was less sensitive to heat, urea and dicumarol. Furthermore, the study showed that the NAD (P) H-linked enzyme was a flavoenzyme which could be inactivated by dialysis against 1 M potassium bromide and reactivated by FMN.

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