期刊论文详细信息
FEBS Letters | |
Reconstitution of a Mg‐ATP‐dependent protein phosphatase and its activation through a phosphorylation mechanism | |
Resink, Therese J.1  Hemmings, Brian A.1  Cohen, Philip1  | |
[1] Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee, DD1 4HN, Scotland | |
关键词: Protein phosphatase-1; Glycogen synthase kinase; Inhibitor-2; Phosphorylase; Thiophosphorylation; | |
DOI : 10.1016/0014-5793(82)80760-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
A Mg-ATP-dependent protein phosphatase has been reconstituted from the catalytic subunit of protein phosphatase-1 and inhibitor-2, and consists of a 1:1 complex between these proteins. Activation of this enzyme by glycogen synthase kinase-3 and Mg-ATP results from the phosphorylation of inhibitor-2 on a threonine residue(s) and is accompanied by the dissociation of the complex. The results prove that protein phosphatase-1 and the Mg-ATP-dependent protein phosphatase contain the same catalytic subunit, and that they are interconvertible forms of the same enzyme.
【 授权许可】
Unknown
【 预 览 】
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