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Distinct Physiological Functions of Thiol Peroxidase Isoenzymes in Saccharomyces cerevisiae*
Based on kinetic properties of five isoforms, their subcellular localizations, and distinct physiology of each null mutant, the physiological functions of five types of TPx isoenzymes in yeast throughout the full growth cycle are discussed. Expand
Thioredoxin-dependent Hydroperoxide Peroxidase Activity of Bacterioferritin Comigratory Protein (BCP) as a New Member of the Thiol-specific Antioxidant Protein (TSA)/Alkyl Hydroperoxide Peroxidase C
Data suggest that Escherichia coli bacterioferritin comigratory protein is a new member of thioredoxin-dependent TSA/AhpC family, acting as a general hydroperoxide peroxidase. Expand
The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system.
This report describes the isolation and purification of a soluble protein from Saccharomyces cerevisiae, which specifically inhibits the inactivation of various enzymes by a nonenzymatic Fe3+/O2/thiol mixed-function oxidase system and proposes that the protector protein functions as a sulfur radical scavenger. Expand
Thioredoxin-linked "Thiol Peroxidase" from Periplasmic Space of Escherichia coli(*)
Three different molecular masses (24, 22, and 20 kDa) of antioxidant proteins were purified in Escherichia coli. These proteins exhibited the preventive effects against the inactivation of glutamineExpand
Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo.
  • Y. Lim, M. Cha, +4 authors I. H. Kim
  • Chemistry, Medicine
  • Biochemical and biophysical research…
  • 15 April 1993
Observations suggest that the sulfhydryl of cysteine in PRP could function as a strong nucleophile to attack and destroy H2O2 and .OH. Expand
Induction of an antioxidant protein of Saccharomyces cerevisiae by O2, Fe3+, or 2-mercaptoethanol.
The results suggest that in vivo induction in yeast of the 27-kDa protein may represent an adaptive response that evolved to protect cells against damage caused by thiol-dependent mixed-function oxidation systems, and the antioxidant protein is conserved in mammalian tissues. Expand
Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae.
The isolated and sequenced a yeast genomic DNA fragment that encodes thiol-specific antioxidant (TSA), and it is suggested that TSA is a physiologically important antioxidant. Expand
Mutation and Mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family
Results suggest that the members of the thiol Px family, including E. coli thiolPx, have a functional cysteine residue and function in vivo as peroxidases. Expand
Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane.
It is suggested that hTSA1 can act as a very effective antioxidant to remove oxidative stresses not only in matrix as a free form but also in the membrane surface of red blood cells (RBC) as a membrane-associated form. Expand
Identification of promoter in the 5'-flanking region of the E. coli thioredoxin-linked thiol peroxidase gene: evidence for the existence of oxygen-related transcriptional regulatory protein.
Northern hybridization showed that expression of tpx gene is regulated at the transcriptional level, and DNA binding assays using inverted repeat sequence including -35 region provides preliminary evidence that expression in E. coli requires additional transcriptional factor in response to oxygen stress. Expand