Occurrence of the methylglyoxal bypass in halophilic Archaea

Aharon Oren*, Peter Gurevich

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Eight species of halophilic Archaea were tested for the presence of the enzymes of the methylglyoxal bypass. Methylglyoxal synthase was found in extracts of all species tested, with the exception of Halobacterium salinarium and Halobacterium cutirubrum. The enzyme of Haloferax volcanii was most active at pH 7 in the absence of salt, and in the presence of 3 M NaCl or KCl activity was half of that without salt, and was inhibited by phosphate. Glyoxalase I was detected in all species tested. Optimal activity of H. volcanii glyoxalase I was found at pH 7 and 3 M KCl; in the absence of salt, activity was strongly reduced. Glutathione could be replaced by γ-glutamylcysteine as the acceptor of the D-lactoyl group. The work shows that the methylglyoxal bypass may be operative in representatives of the archaeal kingdom.

Original languageAmerican English
Pages (from-to)83-87
Number of pages5
JournalFEMS Microbiology Letters
Issue number1
StatePublished - 1 Jan 1995

Bibliographical note

Funding Information:
We thank Gerhard Gottschalk (GBttingen) for invaluable discussions. This work was supported by grants from the Ministry of Science and Culture, Land Niedersachsen,a nd the Israel Science Foundation administred by the Israel Academy of Sciences and Humanities.


  • Archaea
  • Glyoxalase I
  • Halophilic archaea
  • Methylglyoxal synthase
  • γ-Glutamylcysteine


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