guanylate cyclase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: GTP = 3',5'-cyclic GMP + diphosphate. [EC:4.6.1.2]

Guanylate cyclase activity is a crucial enzymatic function involved in the synthesis of cyclic guanosine monophosphate (cGMP), a ubiquitous second messenger molecule that plays a vital role in diverse cellular signaling pathways. This enzymatic process involves the conversion of guanosine triphosphate (GTP) into cGMP, a reaction catalyzed by guanylate cyclases. These enzymes are typically transmembrane proteins with a cytoplasmic catalytic domain and an extracellular ligand-binding domain. When a specific ligand, such as nitric oxide (NO), binds to the extracellular domain, it triggers a conformational change that activates the catalytic domain. The activated enzyme then catalyzes the conversion of GTP to cGMP, leading to the downstream activation of cGMP-dependent protein kinases (PKG) and other downstream signaling pathways. cGMP, in turn, modulates various cellular functions, including smooth muscle relaxation, neurotransmission, phototransduction, and cell proliferation. Guanylate cyclase activity is thus essential for regulating a wide range of physiological processes, including blood pressure control, vision, and neuronal signaling.'
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Proteins (5)

Compounds (8)