Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal

Drug Metabol Drug Interact. 2008;23(1-2):29-50. doi: 10.1515/dmdi.2008.23.1-2.29.

Abstract

The glyoxalase system consists of two enzymes, glyoxalase I and glyoxalase II. This system is important in the detoxification of methylglyoxal. Detailed studies have determined that the glyoxalase I from Escherichia coli, Neisseria meningitidis and Yersinia pestis are maximally activated by Ni2+ and Co2+, and are inactive with Zn2+, a situation quite different from the human glyoxalase I enzyme, which is activated by Zn2+. Recent studies on the Pseudomonas aeruginosa genome have led to the characterization of three different glyoxalase I enzymes, two of which follow a Ni2+/Co2+ activation profile and the third exhibits a human-like preference for Zn2+.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Escherichia coli / enzymology
  • Humans
  • Hydroxyacylglutathione Hydrolase
  • Lactoylglutathione Lyase / genetics
  • Lactoylglutathione Lyase / physiology*
  • Molecular Sequence Data
  • Pseudomonas aeruginosa / enzymology
  • Pyruvaldehyde / metabolism*
  • Sequence Alignment
  • Species Specificity
  • Thiolester Hydrolases / genetics
  • Thiolester Hydrolases / physiology*

Substances

  • Lactoylglutathione Lyase
  • Pyruvaldehyde
  • Thiolester Hydrolases
  • Hydroxyacylglutathione Hydrolase