Serine/threonine protein phosphatases in Dictyostelium discoideum: no evidence for type I activity.
Extracts from Dictyostelium discoideum contain type 2A and 2C serine/threonine-specific protein phosphatases with properties very similar to those from mammals according to their sensitivity to okadaic acid and to their dependence for divalent cations. In contrast, no type 1 protein phosphatase is found at any time of development, neither in the cytosolic nor in the particulate fraction, using glycogen phosphorylase a, casein, histone or the non-proteinous 4-Methylumbelliferyl phosphate as substrates. Both type 2A and 2C protein phosphatase activities remain constant throughout the development cycle.
Simon
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MN
Departamento de Bioquimica, Instituto de Quimica, Universidade de Sao Paulo, Brazil.
Winckler
T
T
Mutzel
R
R
Véron
M
M
da Costa Maia
J C
JC
D000818:Animals; D002413:Cations, Divalent; D002462:Cell Membrane / Q000201:enzymology; D002846:Chromatography, Affinity; D003600:Cytosol / Q000201:enzymology; D004023:Dictyostelium / Q000201:enzymology*; D004988:Ethers, Cyclic / Q000494:pharmacology; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D010761:Phosphorus Radioisotopes
D002413:Cations, Divalent; D004988:Ethers, Cyclic; D007527:Isoenzymes; D010761:Phosphorus Radioisotopes; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases