Adenylate cyclase of Mytilus galloprovincialis posterior adductor muscle: basal properties and sensitivity to serotonin

The presence and characteristics of a membrane-bound adenylate cyclase from Mytilus galloprovincialis Lmk posterior adductor muscle have been investigated. The enzyme has a Michaelis constant (K _m) of 0.38 mM at 20°C and requires divalent cations (Mg²⁺/Mn²⁺) for its activity. Optimal GTP concentrations are between 10^-5 and 10^-4 M. The non-hydrolizable GTP-analogues GMPpNHp and GTPS increase the activity of the enzyme four- to ten-fold. Sodium fluoride stimulates the enzymatic activity seven- to eight-fold. Forskolin increases the enzymatic activity two- to three-fold. Serotonin stimulates the adenylate cyclase activity in a dose-dependent manner. These experiments were performed with mussels collected from the estuary of Muros, Spain, in 1990.