A possible S ‐glutathionylation of specific proteins by glyoxalase II: An in vitro and in silico study

This study suggests that glyoxalase II, through a specific interaction of its catalytic site with target proteins, could be able to perform a rapid and specific protein S‐glutathionylation using its natural substrate S‐d‐lactoylglutathione.
SignificanceThis article reports for the first time a possible additional role of Glo2 that, after interacting with a target protein, is able to promote S‐glutathionylation using its natural substrate SLG, a glutathione derived compound. In this perspective, Glo2 can play a new important regulatory role inS‐glutathionylation, acquiring further significance in cellular post‐translational modifications of proteins.

Source: Cell Biochemistry and Function - December 8, 2016 Category: Biochemistry Authors: Luisa Ercolani, Andrea Scir è, Roberta Galeazzi, Luca Massaccesi, Laura Cianfruglia, Adolfo Amici, Francesco Piva, Lorena Urbanelli, Carla Emiliani, Giovanni Principato, Tatiana Armeni Tags: RESEARCH ARTICLE Source Type: research