Tautomycin from the bacterium Streptomyces verticillatus

FEBS Letters

MacKintosh, Carol¹  Klumpp, Susanne² 

[1] Department of Biochemistry, University of Dundee, Dundee, Scotland, UK;Pharmaceutisches Institut der Universität Tübingen, Tübingen, FRG

关键词: Tautomycin;    Okadaic acid;    Microcystin;    Protein phosphatase;    Tumour promoter;   

DOI  :  10.1016/0014-5793(90)80828-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tautomycin inhibited the catalytic subunits of protein phosphatase-1 (K _{i app} = 0.16 nM) more potently than protein phosphatase 2A (K _{i app} = 0.4 nM), and the native forms of these enzymes in mammalian, protozoan and plant extracts were inhibited in a similar manner. Protein phosphatase 2B was inhibited 10 000-fold less potently, while two other phosphatases and six protein kinases were unaffected at 10 μM. Okadaic acid prevented the binding of tautomycin to protein phosphatase 2A, indicating a common binding site for both inhibitors. The different relative potencies of tautomycin and okadaic acid for protein phosphatases 1 and 2A suggest that parallel use of both inhibitors may help to identify physiological substrates for each enzyme.

【 授权许可】

Unknown