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

TitleDeciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli.
Publication TypeJournal Article
Year of Publication2015
AuthorsReiger, M, Lassak, J, Jung, K
JournalFEMS Microbiol Lett
Volume362
Issue2
Pagination1-7
Date Published2015 Jan
ISSN1574-6968
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.

DOI10.1093/femsle/fnu014
Alternate JournalFEMS Microbiol. Lett.