Tautomycetin Is a Novel and Specific Inhibitor of Serine/Threonine Protein Phosphatase Type 1, PP1
| Autor: | Nobuyasu Matsuura, Shinya Mitsuhashi, Kunimi Kikuchi, Hiroshi Shima, Makoto Ubukata, Hideaki Oikawa |
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| Rok vydání: | 2001 |
| Předmět: |
Antifungal Agents
Phosphoric monoester hydrolases Phosphatase Biophysics Biology Biochemistry Streptomyces Serine chemistry.chemical_compound Phosphoprotein Phosphatases Animals Enzyme Inhibitors Threonine Furans Molecular Biology chemistry.chemical_classification Dose-Response Relationship Drug Brain Cell Biology Protein phosphatase 2 biology.organism_classification Lipids Molecular biology Phosphoric Monoester Hydrolases Rats Enzyme chemistry Tautomycin |
| Zdroj: | Biochemical and Biophysical Research Communications. 287:328-331 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2001.5596 |
| Popis: | Here we isolated tautomycetin, TC, and examined its phosphatase inhibitory activity. Recently we have reported that the left-hand moiety of tautomycin, TM, and the right one containing the spiroketal are essentially required for inhibition of protein phosphatase, PP, and induction of apoptosis, respectively. TC is structurally almost identical to TM except that TC is lacking the spiroketal, which has the potential apoptosis-inducing activity. TC specifically inhibited PP1 activity, IC50 values for purified PP1 and PP2A enzymes being 1.6 and 62 nM, respectively, whereas the IC50 values of TM were 0.21 and 0.94 nM, respectively. These results demonstrate that TC is the most specific PP1 inhibitor out of over 40 species of natural phosphatase inhibitors reported, strongly suggesting that TC is a novel powerful tool to elucidate the physiological roles of PP1 in various biological events. |
| Databáze: | OpenAIRE |
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