title: Purification and partial characterization of two azoreductases from Shigella dysenteriae type 1.
abstract: Two azoreductases (I and II) were purified to homogeneity from extracts of Shigella dysenteriae (type 1). Azoreductase I was a dimer of identical subunits of M(r) 28,000, whereas azoreductase II was a monomer of 11,000 M(r). Both were flavoproteins, each containing 1 mol of FMN per mol enzyme. Both NADH and NADPH functioned as electron donors for the azoreductases. Azoreductase I used Ponceau SX, Tartrazine, Amaranth and Orange II as substrates. Azoreductase II utilized all the dyes except Amaranth.
authors.affiliation: Department of Biochemistry, University College of Science, Calcutta, India.
authors.forename: D K
authors.initials: DK
authors.lastname: Ghosh
authors.forename: A
authors.initials: A
authors.lastname: Mandal
authors.forename: J
authors.initials: J
authors.lastname: Chaudhuri
mesh_terms: D001391:Azo Compounds; D004396:Coloring Agents; D005415:Flavins / Q000494:pharmacology; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D009601:Nitroreductases; D012762:Shigella dysenteriae / Q000145:classification / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D001391:Azo Compounds; D004396:Coloring Agents; D005415:Flavins; D009243:NAD; D009249:NADP; D009247:NADH, NADPH Oxidoreductases; D009601:Nitroreductases; C021106:azoreductase