Isolation and properties of cyclic AMP-dependent protein kinase from Dictyostelium discoideum.
Cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) in Dictyostelium discoideum was shown to be developmentally controlled. No activity was measured in vegetative cells, but activity increased rapidly during differentiation. A simple procedure for the isolation of the catalytic subunit of the kinase from aggregating cells is presented. The cyclic AMP-dependent holoenzyme could be reconstituted by adding purified D. discoideum cyclic AMP-binding protein. Molecular weight, kinetic parameters, pH dependence and affinity for cyclic AMP were determined for the enzyme. Most properties are similar to those of cyclic AMP-dependent kinase from mammalian cells.
D002454:Cell Differentiation; D000242:Cyclic AMP / Q000378:metabolism; D004023:Dictyostelium / Q000201:enzymology* / Q000254:growth & development; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D011494:Protein Kinases / Q000302:isolation & purification*
D009842:Oligopeptides; C037642:kemptide; D000242:Cyclic AMP; D011494:Protein Kinases