A metabolically stable tight-binding transition-state inhibitor of glyoxalase-I

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The design, synthesis, and enzyme kinetics evaluation of a transition-state inhibitor of glyoxalase-I is described. The union of the hydroxamic acid zinc-chelator with a urea isostere for the glu-cys amide bond led to a glutathione analog which retained inhibitory potency toward glyoxalase-I while possessing resistance toward γ-glutamyltranspeptidase mediated breakdown. This compound is viewed as a potential lead for the development of second-generation glyoxalase-I inhibitors wherein, the problems pertaining to metabolism and selectivity are overcome.

Original languageEnglish (US)
Pages (from-to)6039-6042
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number23
StatePublished - Dec 1 2006

Bibliographical note

Copyright 2008 Elsevier B.V., All rights reserved.


  • Glutathione
  • Glyoxalase
  • Hydroxamic acid
  • Methylglyoxal
  • Transition-state inhibitor
  • γ-Glutamyltranspeptidase


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