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PKG inhibitors and activators act on protein kinase G (PKG), a kinase switched on by cyclic nucleotides. A kinase activated by guanosine 3',5'-monophosphate (cGMP) was isolated and partially purified in 1970. Nitric oxide and natriuretic peptides raise cGMP, which binds the regulatory domain of PKG and releases its kinase activity. Mice lacking PKG type I showed defective regulation of vascular and intestinal smooth muscle in a 1998 study. KT 5823 and the cGMP analog Rp-8-Br-PET-cGMPS inhibit PKG, while Sp-8-pCPT-cGMPS activates it. MBP146-78 targets the PKG of apicomplexan parasites such as Toxoplasma. Several compounds, for example A-3 Hydrochloride, also inhibit the related protein kinase A (PKA).
