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, 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.  

Campus Movie 2020

CIPSM Movie

Campus Movie 2012

CIPSM Movie
LMUexcellent
TU München
MPG
Helmholtz München
MPI of Neurobiology
MPI of Biochemistry