ArticleBiochemistry2026
Sirtuin 2 Regulates Histone Glycation as a Semi-deglycase.
Article in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
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Abstract
Methylglyoxal (MGO) and glyoxal (GO) are reactive carbonyl species (RCS) generated as side products in glycolysis and carbohydrate, protein, and fat catabolism, which are enriched in most cancer cells. MGO/GO-induced nonenzymatic glycation on histones plays pathophysiologically important roles in regulating the three-dimensional architecture of cellular chromatin and cancer development. In our previous studies, we have uncovered that enzymes DJ-1 and PAD4 exhibit "glyoxalase" and "deglycase" activities to antagonize the MGO/GO-modifications of histones. We also found that the general inhibition of histone deacetylases using suberoylanilide hydroxamic acid (SAHA) antagonized histone MGO-glycation due to the direct competition of reactive sites (i.e., lysine residues). Here, we report that a histone deacetylase, sirtuin 2 (SIRT2), functions as a "semi-deglycase" that removes lactic and glycolic acids from ε-
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