Background: The glyoxalase enzyme system is a critical component in the detoxification
of cellular metabolically generated alpha-ketoaldehydes, such as methylglyoxal. Inhibitors of these
enzymes have been shown to have potential in the development of antimicrobial and antitumor
agents. A number of glyoxalase I (Glo1) metalloenzymes have been identified and have been
categorized as either Zn2+-activated or Ni2+-activated metalloenzymes.
Method: In the current work, four Glo1 from both metal activation classes and also having different
quaternary structures were screened against two prototypic hydroxamate-containing peptide
inhibitors in order to provide preliminary information on inhibition characteristics for these diverse
Conclusion: This information should prove useful in future inhibitor design initiatives to develop
more potent and organism selective Glo1 inhibitors.
Keywords: Glyoxalase, nickel, zinc, inhibitor, hydroxamate, metalloenzyme, Clostridium, Pseudomonas, Saccharomyces.
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