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Hydroxamate Inhibitor Profiling of Both Zn2+- and Ni2+-Activated Glyoxalase I Metalloenzymes Having Diverse Quaternary Structures

[ Vol. 14 , Issue. 7 ]


Uthaiwan Suttisansanee and John F. Honek*   Pages 843 - 852 ( 10 )


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 metalloenzymes.

Conclusion: This information should prove useful in future inhibitor design initiatives to develop more potent and organism selective Glo1 inhibitors.


Glyoxalase, nickel, zinc, inhibitor, hydroxamate, metalloenzyme, Clostridium, Pseudomonas, Saccharomyces.


Institute of Nutrition, Mahidol University, 25/25 Phutthamonthon 4 Rd., Salaya, Phutthamonthon, Nakhon Pathom 73170, Department of Chemistry, University of Waterloo, 200 University Avenue West, Waterloo, Ontario, Canada N2L 3G1

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