Add time:09/03/2019         Source:sciencedirect.com

The diastereomeric GSH derivatives γ-L-Glu-L-allo-thioThr-Gly (6) and γ-L-Glu-L-thioThr-Gly (6a) have been synthesized as specific probes of the steric environment near the cysteinyl residue of enzyme bound glutathionyl substrates. Experiments with glyoxalase I indicate that while 6a-methylglyoxal thiohemiacetal is a substrate for the enzyme, 6-methylglyoxal thiohemiacetal forms a tight-binding abortive complex with the active site (Ki ⋍ 100 μM). Apparently, the small size of the cysteinyl Cβ-Hs proton of the normal GSH-methylglyoxal thiohemiacetal substrate for glyoxalase I is a strict requirement for productive substrate binding. These compounds may provide a novel approach to the inhibition of GSH-dependent enzymes.

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