ArticleJournal of enzyme inhibition and medicinal chemistry2012
Divergent effects of compounds on the hydrolysis and transpeptidation reactions of γ-glutamyl transpeptidase.
Article in Journal of enzyme inhibition and medicinal chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Transcriptional Activity of Genes Related to the Biotransformation Process in the Development of Colorectal Cancer.International journal of molecular sciences · 2025Article
- GSH and Ferroptosis: Side-by-Side Partners in the Fight against Tumors.Antioxidants (Basel, Switzerland) · 2024Review
- Article
- Structure of 6-diazo-5-oxo-norleucine-bound human gamma-glutamyl transpeptidase 1, a novel mechanism of inactivation.Protein science : a publication of the Protein Society · 2017Article
- Lens glutathione homeostasis: Discrepancies and gaps in knowledge standing in the way of novel therapeutic approaches.Experimental eye research · 2017Review
- Gamma-glutamyl transpeptidase: redox regulation and drug resistance.Advances in cancer research · 2014Review
- Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.The Journal of biological chemistry · 2013Article
- Inhibition of human γ-glutamyl transpeptidase: development of more potent, physiologically relevant, uncompetitive inhibitors.The Biochemical journal · 2013Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
A novel class of inhibitors of the enzyme γ-glutamyl transpeptidase (GGT) were evaluated. The analog OU749 was shown previously to be an uncompetitive inhibitor of the GGT transpeptidation reaction. The data in this study show that it is an equally potent uncompetitive inhibitor of the hydrolysis reaction, the primary reaction catalyzed by GGT in vivo. A series of structural analogs of OU749 were evaluated. For many of the analogs, the potency of the inhibition differed between the hydrolysis and transpeptidation reactions, providing insight into the malleability of the active site of the enzyme. Analogs with electron withdrawing groups on the benzosulfonamide ring, accelerated the hydrolysis reaction, but inhibited the transpeptidation reaction by competing with a dipeptide acceptor. Several of the OU749 analogs inhibited the transpeptidation reaction by slow onset kinetics, similar to acivicin. Further development of inhibitors of the GGT hydrolysis reaction is necessary to provide new therapeutic compounds.
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Registered trials
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