568 research outputs found
Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative
AbstractRat glutathione transferase 4-4 catalysed the conjugation of 2-mercaptoethanol with 1-chloro-2,4-dinitrobenzene in the presence of S-methyl-glutathione. The reaction was linearly dependent on enzyme concentration and saturation was seen with respect to both 2-mercaptoethanol and S-methyl-glutathione concentration. High concentrations of S-methyl-gluta-thione were inhibitory. The results suggest that the natural substrate glutathione has two distinct functions in the normal catalytic reaction, (i) induction of a catalytically competent conformation of the enzyme and (ii) provision of the substrate sulfhydryl group in the reaction catalyzed
Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol
The primary structure of monomeric yeast glyoxalase I indicates a gene duplication resulting in two similar segments homologous with the subunit of dimeric human glyoxalase I
Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange
The contribution of the C-terminal sequence to the catalytic activity of GST2, a human Alpha-class glutathione transferase
Kinetic independence of the subunits of cytosolic glutathione transferase from the rat
Paradoxical inhibition of rat glutathione transferase 4-4 by indomethacin explained by substrate-inhibitor-enzyme complexes in a random-order sequential mechanism
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