Abstract
A new ubiquitin-activating enzyme (E1) inhibitor, himeic acid A, was isolated from a culture of marine-derived fungus, Aspergillus sp. The structure was determined by spectroscopic analysis. The formation of an E1-ubiquitin (Ub) intermediate was 65% inhibited by himeic acid A at the concentration of 50 microM, while two new related compounds, himeic acids B and C, showed little inhibitory activity even at 100 microM.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aspergillus / chemistry*
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Enzyme Inhibitors / isolation & purification*
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Enzyme Inhibitors / pharmacology
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Fatty Acids, Unsaturated / isolation & purification
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Fatty Acids, Unsaturated / pharmacology*
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Marine Biology*
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Pyrones / isolation & purification
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Pyrones / pharmacology*
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Spectrometry, Mass, Fast Atom Bombardment
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Ubiquitin-Activating Enzymes / antagonists & inhibitors*
Substances
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Enzyme Inhibitors
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Fatty Acids, Unsaturated
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Pyrones
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himeic acid A
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Ubiquitin-Activating Enzymes