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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Glutathione / analogs & derivatives
  • Glutathione / metabolism
  • Isoenzymes / genetics
  • Isoenzymes / metabolism*
  • Mutation
  • Phylogeny
  • Pyruvaldehyde / metabolism*
  • Pyruvaldehyde / pharmacology
  • Thiolester Hydrolases / genetics
  • Thiolester Hydrolases / metabolism*
  • Vibrio / enzymology
  • Vibrio / genetics

Substances

  • Isoenzymes
  • Pyruvaldehyde
  • Thiolester Hydrolases
  • hydroxyacylglutathione hydrolase
  • Glutathione
  • S-lactoylglutathione