Cyclic AMP-dependent protein kinase from Ustilago maydis.
Ustilago maydis was surveyed for cyclic AMP-dependent protein kinase activity. Using a combination of ion-exchange and molecular filtration techniques, we demonstrate that there is only one form of cyclic AMP-dependent protein kinase in the cytosolic fraction of the fungus. The kinase activity is specifically activated by cyclic AMP and utilizes protamine and kemptide as substrates. Most, if not all, of the cyclic AMP binding detected in the soluble fraction is associated with the protein kinase activity. Cyclic AMP-dependent protein kinase is completely dissociated by cyclic AMP into catalytic and regulatory subunits having an apparent molecular weight of 35 000 daltons as judged by sucrose gradient centrifugation.
D001487:Basidiomycota / Q000201:enzymology*; D002499:Centrifugation, Density Gradient; D000242:Cyclic AMP / Q000494:pharmacology; D008970:Molecular Weight; D011487:Protein Conformation / Q000187:drug effects; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D014588:Ustilago / Q000201:enzymology*
D000242:Cyclic AMP; D011494:Protein Kinases