Properties of 3',5'-cyclic-AMP phosphodiesterase from Paragonimus africanus metacercariae.
3',5'-Cyclic-AMP 5'-nucleotidohydrolase (cAMP phosphodiesterase, EC 3.1.4.17) was partial purified from metacercariae of Paragonimus africanus. The enzyme activity absolutely depends on Mg2 or Mn2+. The pH-optimum of the cAMP phosphidiesterase was found at pH 8.0. The Michaelis constant for cAMP was determined to be 5 X 10(-6) M. Papaverine deoxyadenosine, theophylline and adenosine were found to be competitive inhibitors of the enzyme activity. The inhibitor constants were calculated to be 13 X 10(-6)M, 25 X 10(-5)M, and 35 X 10(-5)M, and 85 X 10(-5)M,respectively. The molecular weight of the cAMP phosphodiesterase was estimated to be about 40 000 by gel filtration.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium; D008345:Manganese; D008970:Molecular Weight; D010238:Paragonimus / Q000201:enzymology*; D010727:Phosphoric Diester Hydrolases; D011687:Purines / Q000494:pharmacology
D011687:Purines; D008345:Manganese; D010727:Phosphoric Diester Hydrolases; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D008274:Magnesium