Cyclic AMP-dependent and -independent protein kinases of the water mold, Blastocladiella emersonii.
Protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) and cyclic adenosine 3',5'-monophosphate binding activities have been identified in zoospore extracts of the water mold Blastocladiella emersonii. More than 75% of these activities is found in the soluble fraction. Soluble protein kinase activity is resolved in three peaks(I, II and III) by DEAE-cellulose chromatography. Peak I is casein dependent and insensitive to cyclic AMP. Peak II is histone dependent and cyclic AMP independent; this enzyme is inhibited by the heat-stable inhibitor from bovine muscle. Peak III utilizes histone as substrate and is activated by cyclic AMP.
D001754:Blastocladiella / Q000201:enzymology*; D003994:Bucladesine / Q000494:pharmacology; D002364:Caseins / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology*; D006152:Cyclic GMP / Q000494:pharmacology; D005658:Fungi / Q000201:enzymology*; D006657:Histones / Q000378:metabolism; D009124:Muscle Proteins / Q000494:pharmacology; D010710:Phosphates / Q000378:metabolism; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D002364:Caseins; D006657:Histones; D009124:Muscle Proteins; D010710:Phosphates; D003994:Bucladesine; D000242:Cyclic AMP; D011494:Protein Kinases; D006152:Cyclic GMP