title: Distribution of Prx-linked hydroperoxide reductase activity among microorganisms.
abstract: Peroxiredoxin (Prx) constitutes a large family of enzymes found in microorganisms, animals, and plants, but the detection of the activities of Prx-linked hydroperoxide reductases (peroxiredoxin reductases) in cell extracts, and the purification based on peroxide reductase activity, have only been done in bacteria and Trypanosomatidae. A peroxiredoxin reductase (NADH oxidase) from a bacterium, Amphibacillus, displayed only poor activities in the presence of purified Prx from Saccharomyces or Synechocystis, while it is highly active in the presence of bacterial Prx. These results suggested that an enzyme system different from that in bacteria might exist for the reduction of Prx in yeast and cyanobacteria. Prx-linked hydroperoxide reductase activities were detected in cell extracts of Saccharomyces, Synechocystis, and Chlorella, and the enzyme activities of Saccharomyces and Chlorella were induced under vigorously aerated culture conditions and intensive light exposure conditions, respectively. Partial purification of Prx-linked peroxidase from the induced yeast cells indicated that the Prx-linked peroxidase system consists of two protein components, namely, thioredoxin and thioredoxin reductase. This finding is consistent with the previous report on its purification based on its protein protection activity against oxidation [Chae et al., J. Biol. Chem., 269, 27670-27678 (1994)]. In this study we have confirmed that Prx-linked peroxidase activity are widely distributed, not only in bacteria species and Trypanosomatidae, but also in yeast and photosynthetic microorganisms, and showed reconstitution of the activity from partially purified interspecies components.
authors.affiliation: Department of Bioscience, Tokyo University of Agriculture, Tokyo, Japan.
authors.forename: Kouji
authors.initials: K
authors.lastname: Takeda
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Nishiyama
authors.forename: Koji
authors.initials: K
authors.lastname: Yoda
authors.forename: Toshihiro
authors.initials: T
authors.lastname: Watanabe
authors.forename: Kaori
authors.initials: K
authors.lastname: Nimura-Matsune
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Mura
authors.forename: Chiyoko
authors.initials: C
authors.lastname: Tokue
authors.forename: Tetzuya
authors.initials: T
authors.lastname: Katoh
authors.forename: Shinji
authors.initials: S
authors.lastname: Kawasaki
authors.forename: Youichi
authors.initials: Y
authors.lastname: Niimura
mesh_terms: D000818:Animals; D001407:Bacillus / Q000201:enzymology; D002457:Cell Extracts; D002696:Chlamydomonas / Q000201:enzymology*; D002708:Chlorella / Q000201:enzymology*; D000458:Cyanobacteria / Q000201:enzymology*; D005420:Flavoproteins / Q000302:isolation & purification / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010544:Peroxidases / Q000302:isolation & purification / Q000378:metabolism*; D054464:Peroxiredoxins; D012440:Saccharomyces / Q000201:enzymology*
chemical_list: D002457:Cell Extracts; D005420:Flavoproteins; D009097:Multienzyme Complexes; D010544:Peroxidases; D054464:Peroxiredoxins; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; C416102:NADH peroxiredoxin oxidoreductase