Inactivation of human placenta glutathione S-transferase by SH/SS exchange reaction with biological disulfides.

  title={Inactivation of human placenta glutathione S-transferase by SH/SS exchange reaction with biological disulfides.},
  author={T. Nishihara and H. Maeda and K. Okamoto and T. Oshida and T. Mizoguchi and T. Terada},
  journal={Biochemical and biophysical research communications},
  volume={174 2},
The oxidized glutathione inhibited the activity of glutathione S-transferase purified from human placenta just through competitive inhibition. On the other hand, cystine and cystamine inactivated the activity by pseudo first-order in low concentrations, accompanying the stoichiometric incorporation of the radioactivity of [14C]-cystine to the enzyme protein until a half mole per one subunit. This and the protective effect of glutathione analogues suggested that the SH/SS exchange reaction… Expand
Role of thioltransferases on the modulation of rat liver S‐adenosylmethionine synthetase activity by glutathione
Increases of 3‐ to 4‐fold in the oxidation constants for both S‐adenosylmethionine synthetase isoenzymes in the presence of protein disulfide isomerase suggested the possibility of a thiol‐disulfide exchange regulatory mechanism for this enzyme in vivo. Expand
Investigation of the active site of human placenta glutathione transferase pi by means of a spin-labelled glutathione analogue.
It is concluded that integrity of the thiolate of Cys-47 is necessary to maintain an active conformation of the enzyme able to efficiently bind glutathione into the active site. Expand
Modulation of 3 alpha-hydroxysteroid dehydrogenase activity by the redox state of glutathione.
Coenzyme (NADP+) completely protected the enzyme from this inactivation by disulfides, but neither of the substrates (androsterone and benzenedihydrodiol) did and the activity of inactivated enzyme was restored by treatment with thiols such as DTT (dithiothreitol) or GSH. Expand
Purification and Characterization of Glutathione-S-Transferase from Chicken Erythrocyte
  • T. Aydemir, D. Kavrayan
  • Biology, Medicine
  • Artificial cells, blood substitutes, and immobilization biotechnology
  • 2009
The glutathione-s-transferases are a family of multifunctional enzymes involved in the detoxification of electrophilic xenobiotics primarily through conjugation to reduce glutathione. A form of theExpand
Functional Studies of Tyrosine 108 Residue in the Active Site of Human Glutathione S-Transferase P1-1
To gain further insight on the relationship between structure and functions of glutathione S-transferase (GST), the three tyrosine 108 mutants, Y108A, Y108F, and Y108W, of human GST P1-1 wereExpand
Isoenzyme selective irreversible inhibition of rat and human glutathione S-transferases by ethacrynic acid and two brominated derivatives.
It has been shown that ethacrynic acid can inhibit glutathione S-transferase (GST) of the pi-class irreversibly and an active site-directed modification is indicated, suggesting, that a cysteine residue is the target site. Expand
Tyrosine-7 is an essential residue for the catalytic activity of human class PI glutathione S-transferase: chemical modification and site-directed mutagenesis studies.
Tyr7 is considered to be an essential residue for the catalytic activity of GST pi, which is conserved in all cytosolic GSTs, and the replacement of Tyr7 in GST pi with phenylalanine by site-directed mutagenesis lowered the activities toward CDNB and ethacrynic acid. Expand
Pig lens glutathione S-transferase belongs to class Pi enzyme.
Class Pi glutathione S-transferase was purified to homogeneity from pig lens cytosol and Amino acid sequence of N-terminal 15 residues was almost identical to class Pi enzymes from human, rat and mouse. Expand
The Structures of Human Glutathione Transferase P1-1 in Complex with Glutathione and Various Inhibitors at High Resolution
The human pi-class glutathione S-transferase (hGST P1-1) is a target for structure-based inhibitor design with the aim of developing drugs that could be used as adjuvants in chemotherapeuticExpand
The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution.
The structure provides an explanation as to why this compound inhibits the pi-class GST much better than the other GST classes. Expand


Molecular and catalytic properties of purified glutathione S-transferase from human placenta.
Glutathione S-transferase from human placenta has been purified with a simple and rapid method and the steady-state kinetics follow Michaelis-Menten kinetics and the conjugation reaction with 1-chloro-2,4-dinitrobenzene displays a random sequential mechanism. Expand
Glutathione S-transferases. The first enzymatic step in mercapturic acid formation.
The purification of homogeneous glutathione S-transferases B and C from rat liver is described, and only transferases A and C are immunologically related. Expand
Nonequivalence of the two subunits of horse erythrocyte glutathione transferase in their reaction with sulfhydryl reagents.
All the structural and kinetic data reported in this paper indicate a nonsymmetrical association of two identical subunits, or alternatively heterodimeric structure with subunits of very similar charge and size. Expand
Specific inactivation of glutathione S-transferases in class Pi by SH-modifiers.
The present results suggest that the 47th cysteine residue may be located in the vicinity of the active site of Class Pi GSTs, and may be preferentially modified. Expand
The binding of substrates and a product of the enzymatic reaction to glutathione S-transferase A.
The binding studies are fully consistent with a steady state random kinetic mechanism for the glutathione S-transferase A, and all ligands showed the same binding stoichiometry. Expand
Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization, and preliminary crystallographic analysis of a neutral class PI enzyme.
A method was developed to purify glutathione transferase from bovine placenta by affinity chromatography and fast protein liquid chromatography. The purified enzyme was homogeneous as judged byExpand
Glutathione transferases--structure and catalytic activity.
The glutathione transferases are recognized as important catalysts in the biotransformation of xenobiotics, including drugs as well as environmental pollutants. Multiple forms exist, and numerousExpand
The glutathione status of cells.
GSH status, the biologically relevant chemistry of GSH, the forms in which GSH can be present within the cell, along with the GSH content of cells and the methods for analysis of this substance are discussed. Expand
Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation.
  • D. Ziegler
  • Chemistry, Medicine
  • Annual review of biochemistry
  • 1985
PERSPECTIVES AND SUMMARY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 306 REGULATION BY THIOL : DISULFIDE EXCHANGE-ANExpand
The isozymes of glutathion transferase
  • 1985