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Cyclic GMP phosphodiesterases (cGMP PDEs) are enzymes that hydrolyze cyclic guanosine monophosphate (cGMP) to 5’-GMP, thereby regulating the intracellular levels of cGMP. The "low Km" designation refers to a high affinity for cGMP, meaning these enzymes can efficiently hydrolyze cGMP even at low substrate concentrations. These enzymes regulate key signaling pathways by controlling the breakdown of intracellular second messengers like cAMP and especially cGMP. Several PDE families can hydrolyze cGMP, but those with high affinity (low Km) for cGMP include: PDE1, PDE2, PDE5, and PDE9. Selective inhibitors of certain low Km phosphodiesterase isoforms have clinical applications, such as PDE3 inhibitors in heart failure and PDE5 inhibitors for erectile dysfunction and pulmonary hypertension.
Inhibition of cGMP hydrolysis, leading to increased intracellular cGMP levels.
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