Abstract
To investigate the role of the amide group of (-)-indolactam-V (1) on PKC binding, we synthesized (-)-indothiolactam-V (2), a new thioamide analogue of 1, by microbial conversion using Streptomyces blastmyceticum. Compounds 2 and 1 showed similar binding affinities to conventional PKCs but 2 had lower affinities to novel PKCs, suggesting that novel PKCs recognize amide modifications more effectively than conventional PKCs.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding, Competitive
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Carcinogens / chemical synthesis*
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Carcinogens / metabolism
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Enzyme Activation
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Indoles / chemical synthesis
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Indoles / metabolism
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Isoenzymes / metabolism
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Lactams / chemical synthesis
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Lactams / metabolism
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Magnetic Resonance Spectroscopy
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Peptide Fragments / metabolism
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Phorbol 12,13-Dibutyrate / metabolism
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Protein Binding
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Protein Kinase C / chemistry
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Protein Kinase C / metabolism*
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Thioamides / chemical synthesis
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Thioamides / metabolism
Substances
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Carcinogens
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Indoles
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Isoenzymes
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Lactams
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Peptide Fragments
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Thioamides
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Phorbol 12,13-Dibutyrate
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indolactam V
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Protein Kinase C