Phosphorylase phosphatase: new horizons for an old enzyme

Front Biosci. 1999 Mar 15:4:D270-85. doi: 10.2741/lee.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcineurin / physiology
  • Carrier Proteins / metabolism
  • Catalytic Domain* / genetics
  • Cloning, Molecular
  • Enzyme Activation
  • Glycogen / metabolism
  • Holoenzymes / isolation & purification
  • Humans
  • Metalloproteins / physiology
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phosphoprotein Phosphatases / chemistry
  • Phosphoprotein Phosphatases / genetics
  • Phosphoprotein Phosphatases / metabolism*
  • Phosphoprotein Phosphatases / physiology
  • Protein Phosphatase 1
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship

Substances

  • Carrier Proteins
  • Holoenzymes
  • Metalloproteins
  • Recombinant Proteins
  • Glycogen
  • Calcineurin
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1