| FEBS Letters | |
| Remarkable similarities between yeast and mammalian protein phosphatases | |
| Stark, Michael J.R.1  Cohen, Philip1  Schelling, Donald L.1  | |
| [1] Department of Biochemistry, University of Dundee, Dundee, Scotland | |
| 关键词: Protein phosphatase; Okadaic acid; Inhibitor protein; Tumor promoter; Protein phosphorylation; (Yeast); | |
| DOI : 10.1016/0014-5793(89)80804-X | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
Protein phosphatase activities in extracts of the yeast Saccharomyces cerevisiae showed remarkable similarities to the mammalian type 1, type 2A and type 2C enzymes. Similarities included their substrate specificities, including selectivity for the α- and β-subunits of muscle phosphorylase kinase, sensitivity toadaic acid and to mammalian inhibitor 1 and inhibitor 2, and requirement for divalent cations. The results suggest that the function and regulation of these enzymes has been highly conserved during evolution and indicate that the improved procedure for identifying and quantitating protein phosphatases [(1989) FEBS Lett. 250, 000-000] may be applicable to all eukaryotic cells.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020292245ZK.pdf | 405KB |
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