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  • Title: A calcium/calmodulin-dependent cyclic adenosine monophosphate phosphodiesterase from Drosophila heads.
    Author: Yamanaka MK, Kelly LE.
    Journal: Biochim Biophys Acta; 1981 May 05; 674(2):277-86. PubMed ID: 6263352.
    Abstract:
    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.
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