title: An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
abstract: The recent determination of the amino acid sequences of the Bacillus megaterium cytochrome P-450 and the flavoprotein component of Salmonella typhimurium NADPH-sulfite reductase revealed that these enzymes contain a flavoprotein moiety remarkably similar to mammalian NADPH-cytochrome P-450 reductase. The presence of this oxidoreductase in these very different enzymes suggests that this flavoprotein arose early in evolution and was utilized as an enzymological building block. The multi-domain structure of the reductase further suggests that it arose through a fusion of genes encoding simple flavin electron-transport proteins.
authors.affiliation: Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor 48109-0606.
authors.forename: T D
authors.initials: TD
authors.lastname: Porter
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001410:Bacillus megaterium / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D005420:Flavoproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D009251:NADPH-Ferrihemoprotein Reductase / Q000235:genetics*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000235:genetics*; D012486:Salmonella typhimurium / Q000201:enzymology / Q000235:genetics*; D050864:Sulfite Reductase (NADPH)
chemical_list: D005420:Flavoproteins; D009251:NADPH-Ferrihemoprotein Reductase; D050862:Oxidoreductases Acting on Sulfur Group Donors; D050864:Sulfite Reductase (NADPH)