Abstract
This report illustrates the complex enzymology of the multisubstrate protein phosphate that reverses most of the cyclic AMP-mediated protein phosphorylation reactions that regulate glycogen metabolism. The activity of the protein phosphatase is controlled in a dual way: it interconverts between an active and an inactive form, while the expression of its activity can furthermore be prevented by a heat-stable protein (inhibitor-1). The interconversion of the mutisubstrate protein phosphatase is made possible by the presence of a modulator protein, which constitutes the enzyme's regulatory subunit, and by the action of an activating protein, the kinase FA, which is responsible for the transition of the enzyme's catalytic subunit into its active conformation.
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Vandenheede, J.R., Yang, SD. & Merlevede, W. Protein phosphatase interconversions. J Protein Chem 3, 157–166 (1984). https://doi.org/10.1007/BF01040497
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DOI: https://doi.org/10.1007/BF01040497