Explaining the inhibition of glyoxalase II by 9-fluorenylmethoxycarbonyl-protected glutathione derivatives.

Direct Demonstration by H.N.M.R. spectrometry of the stereoselectivity of yeast Glyoxalase l towards the Diastereomeric forms of the a-ketoaldehyde - Glutathione Hemithioacetal

Biomimetic catalytic transformation of toxic α-oxoaldehydes to high-value chiral α-hydroxythioesters using artificial glyoxalase I

Glyoxalase I plays a critical role in the enzymatic defence against glycation by catalysing the isomerization of hemithioacetal, formed spontaneously from cytotoxic α-oxoaldehydes and glutathione, to (S)-α-hydroxyacylglutathione derivatives. Upon the hydrolysis of the thioesters catalysed by glyoxalase II, inert (S)-α-hydroxy acids, that is, lactic acid, are then produced. Herein, we demonstrat...

pH dependence of the inhibition of yeast glyoxalase 1 by prophyrins

The human glutathione transferase P1-1 specific inhibitor TER 117 designed for overcoming cytostatic-drug resistance is also a strong inhibitor of glyoxalase I.

gamma-L-Glutamyl-S-(benzyl)-L-cysteinyl-R-(-)-phenylglycine (TER 117) has previously been developed for selective inhibition of human glutathione S-transferase P1-1 (GST P1-1) based on the postulated contribution of this isoenzyme to the development of drug resistance in cancer cells. In the present investigation, the inhibitory effect of TER 117 on the human glyoxalase system was studied. Alth...

Glyoxalase I--structure, function and a critical role in the enzymatic defence against glycation.

Glyoxalase I is part of the glyoxalase system present in the cytosol of cells. The glyoxalase system catalyses the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids. Glyoxalase I catalyses the isomerization of the hemithioacetal, formed spontaneously from alpha-oxoaldehyde and GSH, to S -2-hydroxyacylglutathione derivatives [RCOCH(OH)-SG-->RCH(OH)CO-SG...