title: Oxygen--insensitive nitrofuran reductases in Salmonella typhimurium TA100.
abstract: 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.
mesh_terms: D001051:Apoenzymes / Q000378:metabolism; D003956:Dialysis; D004352:Drug Resistance, Microbial; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D009601:Nitroreductases; D010088:Oxidoreductases / Q000378:metabolism*; D010100:Oxygen / Q000494:pharmacology*; D012486:Salmonella typhimurium / Q000201:enzymology*; D013997:Time Factors; D014508:Urea / Q000494:pharmacology
chemical_list: D001051:Apoenzymes; D009243:NAD; D009249:NADP; D014508:Urea; D010088:Oxidoreductases; C029492:aromatic NADH-dependent nitroreductase; D009601:Nitroreductases; D010100:Oxygen