Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli

FEMS Microbiology Letters, 2014, doi: 10.1093/femsle/fnu014, 362, 2015, 1–7 published on 04.12.2014
FEMS Microbiology Letters, online article
In Escherichia coli, detoxification of methylglyoxal (MG) requires glyoxalases I and II. Glyoxalase I (gloA/GlxI) isomerizes the hemithioacetal, formed spontaneously from MG and glutathione (GSH) to S-lactoylglutathione (SLG), which is hydrolyzed by glyoxalase II (gloB/GlxII) to lactate and GSH. YcbL from Salmonella enterica serovar Typhimurium is an unusual type II glyoxalase whose role in MG detoxification has remained enigmatic. Here we show that YcbL (gloC/GlxII-2) acts as an accessory type II glyoxylase in E. coli. The two isoenzymes have additive effects and ensure maximal MG degradation.  

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