A calcium/calmodulin-dependent cyclic adenosine monophosphate phosphodiesterase from Drosophila heads.
A Ca2+-activated cycl AMP phosphodiesterase from Drosophila melanogaster heads was studied. The enzyme accounted for approx. 40% of the total, soluble cyclic AMP phosphodiesterase activity in heads. After gel filtration, Ca2+ stimulation of the enzyme was no longer apparent, but Ca2+ activation could be restored by the addition of boiled Drosophila extract to the column-fractionated phosphodiesterase. The protein responsible for restoring Ca2+ activation was purified and shown to have some characteristics of calmodulin. In addition, porcine calmodulin was able to activate the Drosophila phosphodiesterase. Thus, the phosphodiesterase-calmodulin system in Drosophila appears analogous to similar systems in mammals.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002850:Chromatography, Gel; D004331:Drosophila melanogaster / Q000201:enzymology*; D051381:Rats; D013552:Swine
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D002118:Calcium