Reconstitution of a Mg-ATP-dependent protein phosphatase and its activation through a phosphorylation mechanism.
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.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D004789:Enzyme Activation; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010764:Phosphorylase Kinase / Q000378:metabolism; D010762:Phosphorylase a / Q000378:metabolism; D010763:Phosphorylase b / Q000378:metabolism; D010766:Phosphorylation; D054645:Protein Phosphatase 1; D011817:Rabbits
D000255:Adenosine Triphosphate; D010762:Phosphorylase a; D010763:Phosphorylase b; D010764:Phosphorylase Kinase; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1