Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli.
Title | Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli. |
Publication Type | Journal Article |
Year of Publication | 2015 |
Authors | Reiger, M, Lassak, J, Jung, K |
Journal | FEMS Microbiol Lett |
Volume | 362 |
Issue | 2 |
Pagination | 1-7 |
Date Published | 2015 Jan |
ISSN | 1574-6968 |
Abstract | 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. |
DOI | 10.1093/femsle/fnu014 |
Alternate Journal | FEMS Microbiol. Lett. |