Publication: Hydroxamate inhibitor profiling of both zn<sup>2+</sup>- and ni<sup>2+</sup>-activated glyoxalase i metalloenzymes having diverse quaternary structures
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Issued Date
2017-01-01
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ISSN
1875628X
15701808
15701808
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2-s2.0-85026624747
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Mahidol University
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SCOPUS
Bibliographic Citation
Letters in Drug Design and Discovery. Vol.14, No.7 (2017), 843-852
Suggested Citation
Uthaiwan Suttisansanee, John F. Honek Hydroxamate inhibitor profiling of both zn<sup>2+</sup>- and ni<sup>2+</sup>-activated glyoxalase i metalloenzymes having diverse quaternary structures. Letters in Drug Design and Discovery. Vol.14, No.7 (2017), 843-852. doi:10.2174/1570180814666161128115808 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/42027
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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
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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.