Format

Send to

Choose Destination
FEMS Microbiol Lett. 2015 Jan;362(2):1-7. doi: 10.1093/femsle/fnu014. Epub 2014 Dec 4.

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

Author information

1
Munich Center for integrated Protein Science (CiPSM) at the Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Martinsried, Germany Institute of Environmental Medicine, UNIKA-T, Neusässer Straße 47, 86156 Augsburg, Germany Faculty of Medicine, Technische Universität München, Ismaningerstr. 22, 81675 Munich, Germany.
2
Munich Center for integrated Protein Science (CiPSM) at the Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Martinsried, Germany.
3
Munich Center for integrated Protein Science (CiPSM) at the Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Martinsried, Germany jung@lmu.de.

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.

KEYWORDS:

VIBHAR_02708; VIBHAR_03213; Vibrio campbellii; gloB; methylglyoxal

PMID:
25670698
DOI:
10.1093/femsle/fnu014
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Silverchair Information Systems Icon for Wiley
Loading ...
Support Center