Phosphodiesterase 1C, calmodulin-dependent 70kDa Adenovirus (Ad-PDE1C)

The cyclic nucleotide phosphodiesterases (PDEs) have an important role to play in the regulation of cyclic nucleotide levels, as PDE activity hydrolyses camp and cGMP [1-5]. The PDEs are a large superfamily of enzymes consisting of eleven discovered isozyme families (PDE1-11) that differ in respect to substrate specificity, subcellular distribution and regulatory properties [2, 3, 6-9]. Of these eleven families, cGMP-activated PDE (PDE3), cAMP-specific PDE (PDE4), and the more recently discovered PDE7 and PDE8 isozymes mainly hydrolyse cAMP. The PDE5, PDE6 and PDE9 isozymes prefer cGMP as a substrate. Calcium/calmodulin-stimulated PDE (PDE1), cGMP-stimulated PDE (PDE2), PDE10 and PDE11 are dual-substrate PDEs that hydrolyse both cAMP and cGMP.