IMR Press / FBL / Volume 4 / Issue 4 / DOI: 10.2741/lee

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Phosphorylase phosphatase: new horizons for an old enzyme
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1 Department Biochemistry and Molecular Biology, New York Medical College, Valhalla, New York, USA
Academic Editor:Norbert Berndt
Front. Biosci. (Landmark Ed) 1999, 4(4), 270–285;
Published: 15 March 1999
(This article belongs to the Special Issue Cellular functions of protein phosphatases)

Protein phosphatase-1, originally studied as phosphorylase phosphatase, is one of the major ser/thr protein phosphatases. It has a long history and a complex enzymology. It consists of a catalytic subunit of 37 kDa, which is bound to a number of different regulatory or targeting subunits. These are believed to restrict its activity to its immediate microenvironment and thus define its specificity, as well as acting to regulate phosphatase activity. The existence of multiple protein phosphatase-1 binding proteins provides the mechanism whereby phosphatase-1 activity can be involved in a diverse range of cellular functions, and reflects a novel strategy for its evolutionary development.

Protein Phosphatase
Okadaic Acid
Phosphorylase Phosphatase
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