The Saccharomyces cerevisiae type 2A protein phosphatase Pph22p is biochemically different from mammalian PP2A

The Saccharomyces cerevisiae type 2A protein phosphatase (PP2A) Pph22p differs from the catalytic subunits of PP2A (PP2Ac) present in mammals, plants and Schizosaccharomyces pombe by a unique N‐terminal extension of approximately 70 amino acids. We have overexpressed S. cerevisiae Pph22p and its N‐t...

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Veröffentlicht in:	European journal of biochemistry 2002-07, Vol.269 (14), p.3372-3382
Hauptverfasser:	Zabrocki, Piotr, Swiatek, Wojciech, Sugajska, Ewa, Thevelein, Johan M., Wera, Stefaan, Zolnierowicz, Stanislaw
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Catalytic Domain Cloning, Molecular Enzyme Inhibitors - pharmacology heterologous expression Humans Liposomes Mammals - genetics Mammals - metabolism Molecular Sequence Data Oxidation-Reduction Phospholipids - pharmacology Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - chemistry Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Phosphorylase a - metabolism Pichia Pichia pastoris Polylysine - pharmacology Protamines - pharmacology Protein Phosphatase 2 protein phosphatase 2A protein phosphatase Pph22p Protein Structure, Tertiary Recombinant Fusion Proteins - antagonists & inhibitors Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Recombination, Genetic Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - antagonists & inhibitors Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sequence Alignment Sequence Deletion Sequence Homology, Amino Acid Species Specificity Substrate Specificity
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