Uthaiwan SuttisansaneeJohn F. HonekUniversity of WaterlooMahidol University2018-12-212019-03-142018-12-212019-03-142017-01-01Letters in Drug Design and Discovery. Vol.14, No.7 (2017), 843-8521875628X157018082-s2.0-85026624747https://repository.li.mahidol.ac.th/handle/123456789/42027© 2017 Bentham Science Publishers 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.2174/1570180814666161128115808