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|Title:||Hydroxamate inhibitor profiling of both zn<sup>2+</sup>- and ni<sup>2+</sup>-activated glyoxalase i metalloenzymes having diverse quaternary structures|
John F. Honek
University of Waterloo
|Keywords:||Biochemistry, Genetics and Molecular Biology|
|Citation:||Letters in Drug Design and Discovery. Vol.14, No.7 (2017), 843-852|
|Abstract:||© 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.|
|Appears in Collections:||Scopus 2016-2017|
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