Abstract
Hydroxamate-containing tripeptide analogs resembling a reactive intermediate in glyoxalase I catalysis were prepared by solution methods and were found to be competitive inhibitors of the enzyme from Saccharomyces cerevisiae. Electronic properties of the hydroxamate functionality as well as those of the expected intermediates in the enzyme-catalyzed reaction were compared.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding, Competitive
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Drug Design
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology
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Hydroxamic Acids / chemical synthesis*
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Hydroxamic Acids / chemistry
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Hydroxamic Acids / pharmacology
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Indicators and Reagents
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Kinetics
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Lactoylglutathione Lyase / antagonists & inhibitors*
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Structure
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Oligopeptides / chemical synthesis*
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Oligopeptides / chemistry
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Oligopeptides / pharmacology
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Saccharomyces cerevisiae / enzymology
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Spectrometry, Mass, Fast Atom Bombardment
Substances
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Enzyme Inhibitors
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Hydroxamic Acids
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Indicators and Reagents
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Oligopeptides
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Lactoylglutathione Lyase