Phosphoprotein phosphatase from yeast and its ribosomal substrate.
Phosphoprotein phosphatase was isolated from yeast postribosomal supernatant and partly characterized. The enzyme preferentially dephosphorylated phospho-casein and acidic ribosomal proteins L44 and L45, the eukaryotic analogues of bacterial proteins L7 and L12. The evidence suggests that this enzyme is not a catalytic subunit of the multifunctional phosphoprotein phosphatase present in most eukaryotic organisms.
D005656:Fungal Proteins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005656:Fungal Proteins; D012269:Ribosomal Proteins; D010749:Phosphoprotein Phosphatases